human fetuin b Search Results


human fetuin b  (Sino Biological)
90
Sino Biological human fetuin b
a. Periodic arrangement of the active site and prodomain are highlighted as yellow in the surface representation of an idealised meprin α helical segment. b. Example curve representing a series of first-order rates (determined by fitting the linear region of fluorescence versus time) at a given meprin concentration. The kcat/Km is determined from this graph for several meprin concentrations and in triplicate c. First order rate constants (k cat /K m ) of meprin α and variants for small fluorogenic peptide cleavage. Oligomeric state does not appear to affect rate of cleavage of small molecule substrate. d. Inhibitory constant (IC 50 ) of meprin α inhibitors. Determined by fitting and normalising the linear region of fluorescence versus time, in the presence of varying amount of inhibitor at a fixed meprin α concentration. e. Globular proteinaceous inhibitor, murine <t>fetuin-B,</t> and small molecule compound 10d were unaffected by oligomeric state. f. Proteolytic stability of meprin α and variants against trypsin and plasmin. Meprin α oligomers were more stable compared to lower-stoichiometric variants. g. Meprin α thermal stability measured by nanoDSF. Meprin α possess superior thermal stability compared to variants that lack either the disulphide bridge (most drastic) or helical interface interactions. All measurements are statistically significant to all others (p<0.0001, ****) unless otherwise indicated.
Human Fetuin B, supplied by Sino Biological, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+fetuin+b/Human+Fetuin-B+%2F+FETUB+Protein/bio_rxiv__2022__03__13__484121-265-2-8
Average 90 stars, based on 1 article reviews
human fetuin b - by Bioz Stars, 2026-08
90/100 stars
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fetuin a  (BioVendor Instruments)
92
BioVendor Instruments fetuin a
a. Periodic arrangement of the active site and prodomain are highlighted as yellow in the surface representation of an idealised meprin α helical segment. b. Example curve representing a series of first-order rates (determined by fitting the linear region of fluorescence versus time) at a given meprin concentration. The kcat/Km is determined from this graph for several meprin concentrations and in triplicate c. First order rate constants (k cat /K m ) of meprin α and variants for small fluorogenic peptide cleavage. Oligomeric state does not appear to affect rate of cleavage of small molecule substrate. d. Inhibitory constant (IC 50 ) of meprin α inhibitors. Determined by fitting and normalising the linear region of fluorescence versus time, in the presence of varying amount of inhibitor at a fixed meprin α concentration. e. Globular proteinaceous inhibitor, murine <t>fetuin-B,</t> and small molecule compound 10d were unaffected by oligomeric state. f. Proteolytic stability of meprin α and variants against trypsin and plasmin. Meprin α oligomers were more stable compared to lower-stoichiometric variants. g. Meprin α thermal stability measured by nanoDSF. Meprin α possess superior thermal stability compared to variants that lack either the disulphide bridge (most drastic) or helical interface interactions. All measurements are statistically significant to all others (p<0.0001, ****) unless otherwise indicated.
Fetuin A, supplied by BioVendor Instruments, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+fetuin+b/Fetuin-B+Human+ELISA/pmc03645917-49-33-34
Average 92 stars, based on 1 article reviews
fetuin a - by Bioz Stars, 2026-08
92/100 stars
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human fetuin b duoset  (R&D Systems)
94
R&D Systems human fetuin b duoset
a. Periodic arrangement of the active site and prodomain are highlighted as yellow in the surface representation of an idealised meprin α helical segment. b. Example curve representing a series of first-order rates (determined by fitting the linear region of fluorescence versus time) at a given meprin concentration. The kcat/Km is determined from this graph for several meprin concentrations and in triplicate c. First order rate constants (k cat /K m ) of meprin α and variants for small fluorogenic peptide cleavage. Oligomeric state does not appear to affect rate of cleavage of small molecule substrate. d. Inhibitory constant (IC 50 ) of meprin α inhibitors. Determined by fitting and normalising the linear region of fluorescence versus time, in the presence of varying amount of inhibitor at a fixed meprin α concentration. e. Globular proteinaceous inhibitor, murine <t>fetuin-B,</t> and small molecule compound 10d were unaffected by oligomeric state. f. Proteolytic stability of meprin α and variants against trypsin and plasmin. Meprin α oligomers were more stable compared to lower-stoichiometric variants. g. Meprin α thermal stability measured by nanoDSF. Meprin α possess superior thermal stability compared to variants that lack either the disulphide bridge (most drastic) or helical interface interactions. All measurements are statistically significant to all others (p<0.0001, ****) unless otherwise indicated.
Human Fetuin B Duoset, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+fetuin+b/Human+Fetuin+B+DuoSet+ELISA/pmc12238098-70-11-14
Average 94 stars, based on 1 article reviews
human fetuin b duoset - by Bioz Stars, 2026-08
94/100 stars
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goat anti human fetuin a  (R&D Systems)
90
R&D Systems goat anti human fetuin a
a. Periodic arrangement of the active site and prodomain are highlighted as yellow in the surface representation of an idealised meprin α helical segment. b. Example curve representing a series of first-order rates (determined by fitting the linear region of fluorescence versus time) at a given meprin concentration. The kcat/Km is determined from this graph for several meprin concentrations and in triplicate c. First order rate constants (k cat /K m ) of meprin α and variants for small fluorogenic peptide cleavage. Oligomeric state does not appear to affect rate of cleavage of small molecule substrate. d. Inhibitory constant (IC 50 ) of meprin α inhibitors. Determined by fitting and normalising the linear region of fluorescence versus time, in the presence of varying amount of inhibitor at a fixed meprin α concentration. e. Globular proteinaceous inhibitor, murine <t>fetuin-B,</t> and small molecule compound 10d were unaffected by oligomeric state. f. Proteolytic stability of meprin α and variants against trypsin and plasmin. Meprin α oligomers were more stable compared to lower-stoichiometric variants. g. Meprin α thermal stability measured by nanoDSF. Meprin α possess superior thermal stability compared to variants that lack either the disulphide bridge (most drastic) or helical interface interactions. All measurements are statistically significant to all others (p<0.0001, ****) unless otherwise indicated.
Goat Anti Human Fetuin A, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+fetuin+b/Human+Fetuin+B+Biotinylated+Antibody/pmc02900916-298-37-41
Average 90 stars, based on 1 article reviews
goat anti human fetuin a - by Bioz Stars, 2026-08
90/100 stars
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elisa kit  (R&D Systems)
94
R&D Systems elisa kit
a. Periodic arrangement of the active site and prodomain are highlighted as yellow in the surface representation of an idealised meprin α helical segment. b. Example curve representing a series of first-order rates (determined by fitting the linear region of fluorescence versus time) at a given meprin concentration. The kcat/Km is determined from this graph for several meprin concentrations and in triplicate c. First order rate constants (k cat /K m ) of meprin α and variants for small fluorogenic peptide cleavage. Oligomeric state does not appear to affect rate of cleavage of small molecule substrate. d. Inhibitory constant (IC 50 ) of meprin α inhibitors. Determined by fitting and normalising the linear region of fluorescence versus time, in the presence of varying amount of inhibitor at a fixed meprin α concentration. e. Globular proteinaceous inhibitor, murine <t>fetuin-B,</t> and small molecule compound 10d were unaffected by oligomeric state. f. Proteolytic stability of meprin α and variants against trypsin and plasmin. Meprin α oligomers were more stable compared to lower-stoichiometric variants. g. Meprin α thermal stability measured by nanoDSF. Meprin α possess superior thermal stability compared to variants that lack either the disulphide bridge (most drastic) or helical interface interactions. All measurements are statistically significant to all others (p<0.0001, ****) unless otherwise indicated.
Elisa Kit, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+fetuin+b/Human+Fetuin+B+DuoSet+ELISA/pmc08492646-98-11-18
Average 94 stars, based on 1 article reviews
elisa kit - by Bioz Stars, 2026-08
94/100 stars
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anti human fetuin mouse monoclonal antibody  (R&D Systems)
90
R&D Systems anti human fetuin mouse monoclonal antibody
a. Periodic arrangement of the active site and prodomain are highlighted as yellow in the surface representation of an idealised meprin α helical segment. b. Example curve representing a series of first-order rates (determined by fitting the linear region of fluorescence versus time) at a given meprin concentration. The kcat/Km is determined from this graph for several meprin concentrations and in triplicate c. First order rate constants (k cat /K m ) of meprin α and variants for small fluorogenic peptide cleavage. Oligomeric state does not appear to affect rate of cleavage of small molecule substrate. d. Inhibitory constant (IC 50 ) of meprin α inhibitors. Determined by fitting and normalising the linear region of fluorescence versus time, in the presence of varying amount of inhibitor at a fixed meprin α concentration. e. Globular proteinaceous inhibitor, murine <t>fetuin-B,</t> and small molecule compound 10d were unaffected by oligomeric state. f. Proteolytic stability of meprin α and variants against trypsin and plasmin. Meprin α oligomers were more stable compared to lower-stoichiometric variants. g. Meprin α thermal stability measured by nanoDSF. Meprin α possess superior thermal stability compared to variants that lack either the disulphide bridge (most drastic) or helical interface interactions. All measurements are statistically significant to all others (p<0.0001, ****) unless otherwise indicated.
Anti Human Fetuin Mouse Monoclonal Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+fetuin+b/Human+Fetuin+B+Antibody/pm18775894-82-39-44
Average 90 stars, based on 1 article reviews
anti human fetuin mouse monoclonal antibody - by Bioz Stars, 2026-08
90/100 stars
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retroviral untagged vector  (OriGene)
90
OriGene retroviral untagged vector
a. Periodic arrangement of the active site and prodomain are highlighted as yellow in the surface representation of an idealised meprin α helical segment. b. Example curve representing a series of first-order rates (determined by fitting the linear region of fluorescence versus time) at a given meprin concentration. The kcat/Km is determined from this graph for several meprin concentrations and in triplicate c. First order rate constants (k cat /K m ) of meprin α and variants for small fluorogenic peptide cleavage. Oligomeric state does not appear to affect rate of cleavage of small molecule substrate. d. Inhibitory constant (IC 50 ) of meprin α inhibitors. Determined by fitting and normalising the linear region of fluorescence versus time, in the presence of varying amount of inhibitor at a fixed meprin α concentration. e. Globular proteinaceous inhibitor, murine <t>fetuin-B,</t> and small molecule compound 10d were unaffected by oligomeric state. f. Proteolytic stability of meprin α and variants against trypsin and plasmin. Meprin α oligomers were more stable compared to lower-stoichiometric variants. g. Meprin α thermal stability measured by nanoDSF. Meprin α possess superior thermal stability compared to variants that lack either the disulphide bridge (most drastic) or helical interface interactions. All measurements are statistically significant to all others (p<0.0001, ****) unless otherwise indicated.
Retroviral Untagged Vector, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+fetuin+b/Fetuin+B+(FETUB)+Human+shRNA+Plasmid+Kit/us09964535-911-10-28
Average 90 stars, based on 1 article reviews
retroviral untagged vector - by Bioz Stars, 2026-08
90/100 stars
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fetub  (OriGene)
90
OriGene fetub
a. Periodic arrangement of the active site and prodomain are highlighted as yellow in the surface representation of an idealised meprin α helical segment. b. Example curve representing a series of first-order rates (determined by fitting the linear region of fluorescence versus time) at a given meprin concentration. The kcat/Km is determined from this graph for several meprin concentrations and in triplicate c. First order rate constants (k cat /K m ) of meprin α and variants for small fluorogenic peptide cleavage. Oligomeric state does not appear to affect rate of cleavage of small molecule substrate. d. Inhibitory constant (IC 50 ) of meprin α inhibitors. Determined by fitting and normalising the linear region of fluorescence versus time, in the presence of varying amount of inhibitor at a fixed meprin α concentration. e. Globular proteinaceous inhibitor, murine <t>fetuin-B,</t> and small molecule compound 10d were unaffected by oligomeric state. f. Proteolytic stability of meprin α and variants against trypsin and plasmin. Meprin α oligomers were more stable compared to lower-stoichiometric variants. g. Meprin α thermal stability measured by nanoDSF. Meprin α possess superior thermal stability compared to variants that lack either the disulphide bridge (most drastic) or helical interface interactions. All measurements are statistically significant to all others (p<0.0001, ****) unless otherwise indicated.
Fetub, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+fetuin+b/Fetuin+B+(FETUB)+Human+siRNA+Oligo+Duplex/us09964535-911-17-28
Average 90 stars, based on 1 article reviews
fetub - by Bioz Stars, 2026-08
90/100 stars
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primary antibody against human fetuin-b gtx112260  (GeneTex)
90
GeneTex primary antibody against human fetuin-b gtx112260
a. Periodic arrangement of the active site and prodomain are highlighted as yellow in the surface representation of an idealised meprin α helical segment. b. Example curve representing a series of first-order rates (determined by fitting the linear region of fluorescence versus time) at a given meprin concentration. The kcat/Km is determined from this graph for several meprin concentrations and in triplicate c. First order rate constants (k cat /K m ) of meprin α and variants for small fluorogenic peptide cleavage. Oligomeric state does not appear to affect rate of cleavage of small molecule substrate. d. Inhibitory constant (IC 50 ) of meprin α inhibitors. Determined by fitting and normalising the linear region of fluorescence versus time, in the presence of varying amount of inhibitor at a fixed meprin α concentration. e. Globular proteinaceous inhibitor, murine <t>fetuin-B,</t> and small molecule compound 10d were unaffected by oligomeric state. f. Proteolytic stability of meprin α and variants against trypsin and plasmin. Meprin α oligomers were more stable compared to lower-stoichiometric variants. g. Meprin α thermal stability measured by nanoDSF. Meprin α possess superior thermal stability compared to variants that lack either the disulphide bridge (most drastic) or helical interface interactions. All measurements are statistically significant to all others (p<0.0001, ****) unless otherwise indicated.
Primary Antibody Against Human Fetuin B Gtx112260, supplied by GeneTex, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+fetuin+b/primary+antibody+against+human+fetuin+b+gtx112260/pm29138227-63-36-41
Average 90 stars, based on 1 article reviews
primary antibody against human fetuin-b gtx112260 - by Bioz Stars, 2026-08
90/100 stars
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human/mouse/rat fetuin b antibody  (Bio-Techne corporation)
90
Bio-Techne corporation human/mouse/rat fetuin b antibody
a. Periodic arrangement of the active site and prodomain are highlighted as yellow in the surface representation of an idealised meprin α helical segment. b. Example curve representing a series of first-order rates (determined by fitting the linear region of fluorescence versus time) at a given meprin concentration. The kcat/Km is determined from this graph for several meprin concentrations and in triplicate c. First order rate constants (k cat /K m ) of meprin α and variants for small fluorogenic peptide cleavage. Oligomeric state does not appear to affect rate of cleavage of small molecule substrate. d. Inhibitory constant (IC 50 ) of meprin α inhibitors. Determined by fitting and normalising the linear region of fluorescence versus time, in the presence of varying amount of inhibitor at a fixed meprin α concentration. e. Globular proteinaceous inhibitor, murine <t>fetuin-B,</t> and small molecule compound 10d were unaffected by oligomeric state. f. Proteolytic stability of meprin α and variants against trypsin and plasmin. Meprin α oligomers were more stable compared to lower-stoichiometric variants. g. Meprin α thermal stability measured by nanoDSF. Meprin α possess superior thermal stability compared to variants that lack either the disulphide bridge (most drastic) or helical interface interactions. All measurements are statistically significant to all others (p<0.0001, ****) unless otherwise indicated.
Human/Mouse/Rat Fetuin B Antibody, supplied by Bio-Techne corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+fetuin+b/Human%2FMouse%2FRat+Fetuin+B+Antibody/bio-techne+corporation___af1725
Average 90 stars, based on 1 article reviews
human/mouse/rat fetuin b antibody - by Bioz Stars, 2026-08
90/100 stars
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recombinant human fetuin a  (R&D Systems)
90
R&D Systems recombinant human fetuin a
a. Periodic arrangement of the active site and prodomain are highlighted as yellow in the surface representation of an idealised meprin α helical segment. b. Example curve representing a series of first-order rates (determined by fitting the linear region of fluorescence versus time) at a given meprin concentration. The kcat/Km is determined from this graph for several meprin concentrations and in triplicate c. First order rate constants (k cat /K m ) of meprin α and variants for small fluorogenic peptide cleavage. Oligomeric state does not appear to affect rate of cleavage of small molecule substrate. d. Inhibitory constant (IC 50 ) of meprin α inhibitors. Determined by fitting and normalising the linear region of fluorescence versus time, in the presence of varying amount of inhibitor at a fixed meprin α concentration. e. Globular proteinaceous inhibitor, murine <t>fetuin-B,</t> and small molecule compound 10d were unaffected by oligomeric state. f. Proteolytic stability of meprin α and variants against trypsin and plasmin. Meprin α oligomers were more stable compared to lower-stoichiometric variants. g. Meprin α thermal stability measured by nanoDSF. Meprin α possess superior thermal stability compared to variants that lack either the disulphide bridge (most drastic) or helical interface interactions. All measurements are statistically significant to all others (p<0.0001, ****) unless otherwise indicated.
Recombinant Human Fetuin A, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+fetuin+b/Recombinant+Human+Fetuin+B+Protein%2C+CF/pm20806899-68-0-6
Average 90 stars, based on 1 article reviews
recombinant human fetuin a - by Bioz Stars, 2026-08
90/100 stars
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human fetuin a  (BioVendor Instruments)
90
BioVendor Instruments human fetuin a
a. Periodic arrangement of the active site and prodomain are highlighted as yellow in the surface representation of an idealised meprin α helical segment. b. Example curve representing a series of first-order rates (determined by fitting the linear region of fluorescence versus time) at a given meprin concentration. The kcat/Km is determined from this graph for several meprin concentrations and in triplicate c. First order rate constants (k cat /K m ) of meprin α and variants for small fluorogenic peptide cleavage. Oligomeric state does not appear to affect rate of cleavage of small molecule substrate. d. Inhibitory constant (IC 50 ) of meprin α inhibitors. Determined by fitting and normalising the linear region of fluorescence versus time, in the presence of varying amount of inhibitor at a fixed meprin α concentration. e. Globular proteinaceous inhibitor, murine <t>fetuin-B,</t> and small molecule compound 10d were unaffected by oligomeric state. f. Proteolytic stability of meprin α and variants against trypsin and plasmin. Meprin α oligomers were more stable compared to lower-stoichiometric variants. g. Meprin α thermal stability measured by nanoDSF. Meprin α possess superior thermal stability compared to variants that lack either the disulphide bridge (most drastic) or helical interface interactions. All measurements are statistically significant to all others (p<0.0001, ****) unless otherwise indicated.
Human Fetuin A, supplied by BioVendor Instruments, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+fetuin+b/Fetuin-B+Human%2C+Sheep+Polyclonal+Antibody/pm20496312-7-18-20
Average 90 stars, based on 1 article reviews
human fetuin a - by Bioz Stars, 2026-08
90/100 stars
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Image Search Results


a. Periodic arrangement of the active site and prodomain are highlighted as yellow in the surface representation of an idealised meprin α helical segment. b. Example curve representing a series of first-order rates (determined by fitting the linear region of fluorescence versus time) at a given meprin concentration. The kcat/Km is determined from this graph for several meprin concentrations and in triplicate c. First order rate constants (k cat /K m ) of meprin α and variants for small fluorogenic peptide cleavage. Oligomeric state does not appear to affect rate of cleavage of small molecule substrate. d. Inhibitory constant (IC 50 ) of meprin α inhibitors. Determined by fitting and normalising the linear region of fluorescence versus time, in the presence of varying amount of inhibitor at a fixed meprin α concentration. e. Globular proteinaceous inhibitor, murine fetuin-B, and small molecule compound 10d were unaffected by oligomeric state. f. Proteolytic stability of meprin α and variants against trypsin and plasmin. Meprin α oligomers were more stable compared to lower-stoichiometric variants. g. Meprin α thermal stability measured by nanoDSF. Meprin α possess superior thermal stability compared to variants that lack either the disulphide bridge (most drastic) or helical interface interactions. All measurements are statistically significant to all others (p<0.0001, ****) unless otherwise indicated.

Journal: bioRxiv

Article Title: Helical ultrastructure of the oncogenic metalloprotease meprin α in complex with a small molecule hydroxamate inhibitor

doi: 10.1101/2022.03.13.484121

Figure Lengend Snippet: a. Periodic arrangement of the active site and prodomain are highlighted as yellow in the surface representation of an idealised meprin α helical segment. b. Example curve representing a series of first-order rates (determined by fitting the linear region of fluorescence versus time) at a given meprin concentration. The kcat/Km is determined from this graph for several meprin concentrations and in triplicate c. First order rate constants (k cat /K m ) of meprin α and variants for small fluorogenic peptide cleavage. Oligomeric state does not appear to affect rate of cleavage of small molecule substrate. d. Inhibitory constant (IC 50 ) of meprin α inhibitors. Determined by fitting and normalising the linear region of fluorescence versus time, in the presence of varying amount of inhibitor at a fixed meprin α concentration. e. Globular proteinaceous inhibitor, murine fetuin-B, and small molecule compound 10d were unaffected by oligomeric state. f. Proteolytic stability of meprin α and variants against trypsin and plasmin. Meprin α oligomers were more stable compared to lower-stoichiometric variants. g. Meprin α thermal stability measured by nanoDSF. Meprin α possess superior thermal stability compared to variants that lack either the disulphide bridge (most drastic) or helical interface interactions. All measurements are statistically significant to all others (p<0.0001, ****) unless otherwise indicated.

Article Snippet: His-tagged recombinant human fetuin-B (11834-H08H) was purchased from SinoBiological.

Techniques: Fluorescence, Concentration Assay, Nano Differential Scanning Fluorimetry

a. Rigid body fit of murine fetuin-B/meprin β crystal structure (PDB 7AUW) to helical structure of meprin α. Arrangement of fetuin-B reveal monomers may pack into a slanted intercalated state that is not significantly prohibited by steric clashes. b. View of a tetramer of fetuin-B based on meprin α docking reveals potential interactions to form a higher-order inhibitory filamentous complex are possible. c. Side view of single fetuin-B dimer forms a “horseshoe” where putative interactions between inter-subunit fetuin-B domains may occur shown in (d), and (e). d, e. Models are not refined, rigid body fitting results in some minor clashes. f. The predicted oligomeric interface corresponds to an evolutionarily conserved interface revealed by ConSurf analysis. g. Side and top views of the cryo-EM reconstruction of human fetuin-B (red) in complex with meprin α (grey, black) at 3.7 Å resolution. Fetuin-B is observed to pack intimately within the meprin α active groove and intercalate as a secondary helix.

Journal: bioRxiv

Article Title: Helical ultrastructure of the oncogenic metalloprotease meprin α in complex with a small molecule hydroxamate inhibitor

doi: 10.1101/2022.03.13.484121

Figure Lengend Snippet: a. Rigid body fit of murine fetuin-B/meprin β crystal structure (PDB 7AUW) to helical structure of meprin α. Arrangement of fetuin-B reveal monomers may pack into a slanted intercalated state that is not significantly prohibited by steric clashes. b. View of a tetramer of fetuin-B based on meprin α docking reveals potential interactions to form a higher-order inhibitory filamentous complex are possible. c. Side view of single fetuin-B dimer forms a “horseshoe” where putative interactions between inter-subunit fetuin-B domains may occur shown in (d), and (e). d, e. Models are not refined, rigid body fitting results in some minor clashes. f. The predicted oligomeric interface corresponds to an evolutionarily conserved interface revealed by ConSurf analysis. g. Side and top views of the cryo-EM reconstruction of human fetuin-B (red) in complex with meprin α (grey, black) at 3.7 Å resolution. Fetuin-B is observed to pack intimately within the meprin α active groove and intercalate as a secondary helix.

Article Snippet: His-tagged recombinant human fetuin-B (11834-H08H) was purchased from SinoBiological.

Techniques: Cryo-EM Sample Prep