Review



codon-optimized nucleotide of wt ccr8  (GenScript corporation)

 
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 90
      Buy from Supplier

    Structured Review

    GenScript corporation codon-optimized nucleotide of wt ccr8
    ( A and B ) Cryo-EM map (A) and cartoon representation of the atomic model (B) of the <t>apo-CCR8-G</t> i (left), LMD-009–CCR8–G i (middle), and ZK 756326–CCR8–G i (right) complexes were shown, respectively. Color coding is annotated for each protein component.
    Codon Optimized Nucleotide Of Wt Ccr8, supplied by GenScript 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/result/codon-optimized nucleotide of wt ccr8/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    codon-optimized nucleotide of wt ccr8 - by Bioz Stars, 2026-06
    90/100 stars

    Images

    1) Product Images from "Unveiling the structural mechanisms of nonpeptide ligand recognition and activation in human chemokine receptor CCR8"

    Article Title: Unveiling the structural mechanisms of nonpeptide ligand recognition and activation in human chemokine receptor CCR8

    Journal: Science Advances

    doi: 10.1126/sciadv.adj7500

    ( A and B ) Cryo-EM map (A) and cartoon representation of the atomic model (B) of the apo-CCR8-G i (left), LMD-009–CCR8–G i (middle), and ZK 756326–CCR8–G i (right) complexes were shown, respectively. Color coding is annotated for each protein component.
    Figure Legend Snippet: ( A and B ) Cryo-EM map (A) and cartoon representation of the atomic model (B) of the apo-CCR8-G i (left), LMD-009–CCR8–G i (middle), and ZK 756326–CCR8–G i (right) complexes were shown, respectively. Color coding is annotated for each protein component.

    Techniques Used: Cryo-EM Sample Prep

    ( A and B ) Overall structure of CCR8-G i complex bound to ZK 756326 (A) or LMD-009 (B), with the orthosteric pocket zoomed in through a sectional view. ( C and E ) Key residues involved in ZK 756326 (C) or LMD-009 (E) binding in CCR8-G i complex structures. The residues involved in interactions are shown as sticks, and hydrogen bonds are highlighted with black dashed lines. ( D and F ) Mutagenesis and functional measurement (G αβγ heterotrimer dissociation by BRET assay) of ZK 756326 (D)– or LMD-009 (F)–induced G i activation of CCR8. Data are shown as means ± SEM from at least three independent experiments performed in technical triplicates.
    Figure Legend Snippet: ( A and B ) Overall structure of CCR8-G i complex bound to ZK 756326 (A) or LMD-009 (B), with the orthosteric pocket zoomed in through a sectional view. ( C and E ) Key residues involved in ZK 756326 (C) or LMD-009 (E) binding in CCR8-G i complex structures. The residues involved in interactions are shown as sticks, and hydrogen bonds are highlighted with black dashed lines. ( D and F ) Mutagenesis and functional measurement (G αβγ heterotrimer dissociation by BRET assay) of ZK 756326 (D)– or LMD-009 (F)–induced G i activation of CCR8. Data are shown as means ± SEM from at least three independent experiments performed in technical triplicates.

    Techniques Used: Binding Assay, Mutagenesis, Functional Assay, Bioluminescence Resonance Energy Transfer, Activation Assay

    ( A to D ) Interactions between conserved Y 1.39 Y 3.32 E 7.39 motif in different CKRs with corresponding chemokines. CCR1-CCL15 (A), CCR2-CCL2 (B), CCR5-CCL15 (C), and CCR5-CCL3 (D). The hydrogen bonds are shown as dashed black line. ( E to H ) Interactions between conserved Y 1.39 Y 3.32 E 7.39 motif in different CKRs with nonpeptide ligands. The hydrogen bonds are shown as dashed black line. CCR2 and RA-[R] (E), CCR5-maraviroc (F), CCR8–LMD-009 (G), and CCR8–ZK 756326 (H). ( I ) Sequence alignment of Y 1.39 Y 3.32 E 7.39 motif and surrounded residues in the 10 human CC CKRs. Y 1.39 , Y 3.32 , and E 7.39 are shown in red, and the structurally equivalent positions are shown with a light blue background.
    Figure Legend Snippet: ( A to D ) Interactions between conserved Y 1.39 Y 3.32 E 7.39 motif in different CKRs with corresponding chemokines. CCR1-CCL15 (A), CCR2-CCL2 (B), CCR5-CCL15 (C), and CCR5-CCL3 (D). The hydrogen bonds are shown as dashed black line. ( E to H ) Interactions between conserved Y 1.39 Y 3.32 E 7.39 motif in different CKRs with nonpeptide ligands. The hydrogen bonds are shown as dashed black line. CCR2 and RA-[R] (E), CCR5-maraviroc (F), CCR8–LMD-009 (G), and CCR8–ZK 756326 (H). ( I ) Sequence alignment of Y 1.39 Y 3.32 E 7.39 motif and surrounded residues in the 10 human CC CKRs. Y 1.39 , Y 3.32 , and E 7.39 are shown in red, and the structurally equivalent positions are shown with a light blue background.

    Techniques Used: Sequencing

    ( A ) Sequence alignment of human CCR8 orthosteric pocket with other nine human CC CKRs. Differential residues are labeled in gray shade. The residue 3.33 and residue 4.64 of CCR8 are shown in red font. ( B and C ) Two key residues in CCR8 for nonpeptide ligand selectivity: Y 3.33 and Y 4.64 . The black dotted lines represent hydrogen bonds. ( D and E ) Functional effect of CCR8 mutation on CCR8 signaling activity was monitored by Ca 2+ flux assay in HEK293 T cells, stimulated by LMD-009 (D) and ZK 756326 (E). Data points represent mean signal ± SD ( n = 3). Data shown are representatives of three independent experiments. Fits to data points by a three-parameter response model are shown as solid lines.
    Figure Legend Snippet: ( A ) Sequence alignment of human CCR8 orthosteric pocket with other nine human CC CKRs. Differential residues are labeled in gray shade. The residue 3.33 and residue 4.64 of CCR8 are shown in red font. ( B and C ) Two key residues in CCR8 for nonpeptide ligand selectivity: Y 3.33 and Y 4.64 . The black dotted lines represent hydrogen bonds. ( D and E ) Functional effect of CCR8 mutation on CCR8 signaling activity was monitored by Ca 2+ flux assay in HEK293 T cells, stimulated by LMD-009 (D) and ZK 756326 (E). Data points represent mean signal ± SD ( n = 3). Data shown are representatives of three independent experiments. Fits to data points by a three-parameter response model are shown as solid lines.

    Techniques Used: Sequencing, Labeling, Residue, Functional Assay, Mutagenesis, Activity Assay, Flux Assay

    ( A ) Agonist-bound CCR8 (active state) structures superimposed on the inactive CCR2 structure (CCR2-BMS681, PDB: 5T1A, green color). ( B ) Agonist-bound CCR8 (active state) structures superimposed on the inactive CCR5 structure (CCR5-maraviroc, PDB: 4MBS, yellow color). ( C to F ) Comparing the conformational changes in the conserved motif between activated CCR8 and inactive CCR2. The movement of F254 6.51 and the downward swing of W251 6.48 are indicated by red arrows. ( G to J ) Comparing the conformational changes in the conserved motif between activated CCR8 and inactive CCR5. LMD-009–bound CCR8 is shown in blue, and ZK 756326–bound CCR8 is shown in gray.
    Figure Legend Snippet: ( A ) Agonist-bound CCR8 (active state) structures superimposed on the inactive CCR2 structure (CCR2-BMS681, PDB: 5T1A, green color). ( B ) Agonist-bound CCR8 (active state) structures superimposed on the inactive CCR5 structure (CCR5-maraviroc, PDB: 4MBS, yellow color). ( C to F ) Comparing the conformational changes in the conserved motif between activated CCR8 and inactive CCR2. The movement of F254 6.51 and the downward swing of W251 6.48 are indicated by red arrows. ( G to J ) Comparing the conformational changes in the conserved motif between activated CCR8 and inactive CCR5. LMD-009–bound CCR8 is shown in blue, and ZK 756326–bound CCR8 is shown in gray.

    Techniques Used:

    ( A ) Overall comparison of three CCR8-G i structures by superposition on CCR8 (left); insertion of the α5-helix (G αi , cyan) into the CCR8 TMD represented as surface (right). ( B ) Molecular interactions between CCR8 and G αi shown in 2D. The interacting residues on G αi and CCR8 are shown in cyan and black, respectively. Residues on 7TM, ICL2, ICL3, and H8 are shown in light blue, pink, yellow, and cyan circles, respectively. Hydrogen bonds are highlighted with dashed red lines. ( C ) Sequence alignment of CCR1, CCR2, CCR3, CCR5, CCR6, and CCR8 in the regions of G protein interface. ( D and E ) Mutagenesis of G protein interface residues and functional measurement (G αβγ heterotrimer dissociation by BRET assay) of ZK 756326 (D)– or LMD-009 (E)–induced G i activation of CCR8. Data are means ± SEM.
    Figure Legend Snippet: ( A ) Overall comparison of three CCR8-G i structures by superposition on CCR8 (left); insertion of the α5-helix (G αi , cyan) into the CCR8 TMD represented as surface (right). ( B ) Molecular interactions between CCR8 and G αi shown in 2D. The interacting residues on G αi and CCR8 are shown in cyan and black, respectively. Residues on 7TM, ICL2, ICL3, and H8 are shown in light blue, pink, yellow, and cyan circles, respectively. Hydrogen bonds are highlighted with dashed red lines. ( C ) Sequence alignment of CCR1, CCR2, CCR3, CCR5, CCR6, and CCR8 in the regions of G protein interface. ( D and E ) Mutagenesis of G protein interface residues and functional measurement (G αβγ heterotrimer dissociation by BRET assay) of ZK 756326 (D)– or LMD-009 (E)–induced G i activation of CCR8. Data are means ± SEM.

    Techniques Used: Comparison, Sequencing, Mutagenesis, Functional Assay, Bioluminescence Resonance Energy Transfer, Activation Assay



    Similar Products

    codon-optimized nucleotide of wt ccr8  (GenScript corporation)
    90
    GenScript corporation codon-optimized nucleotide of wt ccr8
    ( A and B ) Cryo-EM map (A) and cartoon representation of the atomic model (B) of the <t>apo-CCR8-G</t> i (left), LMD-009–CCR8–G i (middle), and ZK 756326–CCR8–G i (right) complexes were shown, respectively. Color coding is annotated for each protein component.
    Codon Optimized Nucleotide Of Wt Ccr8, supplied by GenScript 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/result/codon-optimized nucleotide of wt ccr8/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    codon-optimized nucleotide of wt ccr8 - by Bioz Stars, 2026-06
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    ( A and B ) Cryo-EM map (A) and cartoon representation of the atomic model (B) of the apo-CCR8-G i (left), LMD-009–CCR8–G i (middle), and ZK 756326–CCR8–G i (right) complexes were shown, respectively. Color coding is annotated for each protein component.

    Journal: Science Advances

    Article Title: Unveiling the structural mechanisms of nonpeptide ligand recognition and activation in human chemokine receptor CCR8

    doi: 10.1126/sciadv.adj7500

    Figure Lengend Snippet: ( A and B ) Cryo-EM map (A) and cartoon representation of the atomic model (B) of the apo-CCR8-G i (left), LMD-009–CCR8–G i (middle), and ZK 756326–CCR8–G i (right) complexes were shown, respectively. Color coding is annotated for each protein component.

    Article Snippet: The codon-optimized nucleotide of WT CCR8 (UniProt ID P51685) was synthesized by GenScript.

    Techniques: Cryo-EM Sample Prep

    ( A and B ) Overall structure of CCR8-G i complex bound to ZK 756326 (A) or LMD-009 (B), with the orthosteric pocket zoomed in through a sectional view. ( C and E ) Key residues involved in ZK 756326 (C) or LMD-009 (E) binding in CCR8-G i complex structures. The residues involved in interactions are shown as sticks, and hydrogen bonds are highlighted with black dashed lines. ( D and F ) Mutagenesis and functional measurement (G αβγ heterotrimer dissociation by BRET assay) of ZK 756326 (D)– or LMD-009 (F)–induced G i activation of CCR8. Data are shown as means ± SEM from at least three independent experiments performed in technical triplicates.

    Journal: Science Advances

    Article Title: Unveiling the structural mechanisms of nonpeptide ligand recognition and activation in human chemokine receptor CCR8

    doi: 10.1126/sciadv.adj7500

    Figure Lengend Snippet: ( A and B ) Overall structure of CCR8-G i complex bound to ZK 756326 (A) or LMD-009 (B), with the orthosteric pocket zoomed in through a sectional view. ( C and E ) Key residues involved in ZK 756326 (C) or LMD-009 (E) binding in CCR8-G i complex structures. The residues involved in interactions are shown as sticks, and hydrogen bonds are highlighted with black dashed lines. ( D and F ) Mutagenesis and functional measurement (G αβγ heterotrimer dissociation by BRET assay) of ZK 756326 (D)– or LMD-009 (F)–induced G i activation of CCR8. Data are shown as means ± SEM from at least three independent experiments performed in technical triplicates.

    Article Snippet: The codon-optimized nucleotide of WT CCR8 (UniProt ID P51685) was synthesized by GenScript.

    Techniques: Binding Assay, Mutagenesis, Functional Assay, Bioluminescence Resonance Energy Transfer, Activation Assay

    ( A to D ) Interactions between conserved Y 1.39 Y 3.32 E 7.39 motif in different CKRs with corresponding chemokines. CCR1-CCL15 (A), CCR2-CCL2 (B), CCR5-CCL15 (C), and CCR5-CCL3 (D). The hydrogen bonds are shown as dashed black line. ( E to H ) Interactions between conserved Y 1.39 Y 3.32 E 7.39 motif in different CKRs with nonpeptide ligands. The hydrogen bonds are shown as dashed black line. CCR2 and RA-[R] (E), CCR5-maraviroc (F), CCR8–LMD-009 (G), and CCR8–ZK 756326 (H). ( I ) Sequence alignment of Y 1.39 Y 3.32 E 7.39 motif and surrounded residues in the 10 human CC CKRs. Y 1.39 , Y 3.32 , and E 7.39 are shown in red, and the structurally equivalent positions are shown with a light blue background.

    Journal: Science Advances

    Article Title: Unveiling the structural mechanisms of nonpeptide ligand recognition and activation in human chemokine receptor CCR8

    doi: 10.1126/sciadv.adj7500

    Figure Lengend Snippet: ( A to D ) Interactions between conserved Y 1.39 Y 3.32 E 7.39 motif in different CKRs with corresponding chemokines. CCR1-CCL15 (A), CCR2-CCL2 (B), CCR5-CCL15 (C), and CCR5-CCL3 (D). The hydrogen bonds are shown as dashed black line. ( E to H ) Interactions between conserved Y 1.39 Y 3.32 E 7.39 motif in different CKRs with nonpeptide ligands. The hydrogen bonds are shown as dashed black line. CCR2 and RA-[R] (E), CCR5-maraviroc (F), CCR8–LMD-009 (G), and CCR8–ZK 756326 (H). ( I ) Sequence alignment of Y 1.39 Y 3.32 E 7.39 motif and surrounded residues in the 10 human CC CKRs. Y 1.39 , Y 3.32 , and E 7.39 are shown in red, and the structurally equivalent positions are shown with a light blue background.

    Article Snippet: The codon-optimized nucleotide of WT CCR8 (UniProt ID P51685) was synthesized by GenScript.

    Techniques: Sequencing

    ( A ) Sequence alignment of human CCR8 orthosteric pocket with other nine human CC CKRs. Differential residues are labeled in gray shade. The residue 3.33 and residue 4.64 of CCR8 are shown in red font. ( B and C ) Two key residues in CCR8 for nonpeptide ligand selectivity: Y 3.33 and Y 4.64 . The black dotted lines represent hydrogen bonds. ( D and E ) Functional effect of CCR8 mutation on CCR8 signaling activity was monitored by Ca 2+ flux assay in HEK293 T cells, stimulated by LMD-009 (D) and ZK 756326 (E). Data points represent mean signal ± SD ( n = 3). Data shown are representatives of three independent experiments. Fits to data points by a three-parameter response model are shown as solid lines.

    Journal: Science Advances

    Article Title: Unveiling the structural mechanisms of nonpeptide ligand recognition and activation in human chemokine receptor CCR8

    doi: 10.1126/sciadv.adj7500

    Figure Lengend Snippet: ( A ) Sequence alignment of human CCR8 orthosteric pocket with other nine human CC CKRs. Differential residues are labeled in gray shade. The residue 3.33 and residue 4.64 of CCR8 are shown in red font. ( B and C ) Two key residues in CCR8 for nonpeptide ligand selectivity: Y 3.33 and Y 4.64 . The black dotted lines represent hydrogen bonds. ( D and E ) Functional effect of CCR8 mutation on CCR8 signaling activity was monitored by Ca 2+ flux assay in HEK293 T cells, stimulated by LMD-009 (D) and ZK 756326 (E). Data points represent mean signal ± SD ( n = 3). Data shown are representatives of three independent experiments. Fits to data points by a three-parameter response model are shown as solid lines.

    Article Snippet: The codon-optimized nucleotide of WT CCR8 (UniProt ID P51685) was synthesized by GenScript.

    Techniques: Sequencing, Labeling, Residue, Functional Assay, Mutagenesis, Activity Assay, Flux Assay

    ( A ) Agonist-bound CCR8 (active state) structures superimposed on the inactive CCR2 structure (CCR2-BMS681, PDB: 5T1A, green color). ( B ) Agonist-bound CCR8 (active state) structures superimposed on the inactive CCR5 structure (CCR5-maraviroc, PDB: 4MBS, yellow color). ( C to F ) Comparing the conformational changes in the conserved motif between activated CCR8 and inactive CCR2. The movement of F254 6.51 and the downward swing of W251 6.48 are indicated by red arrows. ( G to J ) Comparing the conformational changes in the conserved motif between activated CCR8 and inactive CCR5. LMD-009–bound CCR8 is shown in blue, and ZK 756326–bound CCR8 is shown in gray.

    Journal: Science Advances

    Article Title: Unveiling the structural mechanisms of nonpeptide ligand recognition and activation in human chemokine receptor CCR8

    doi: 10.1126/sciadv.adj7500

    Figure Lengend Snippet: ( A ) Agonist-bound CCR8 (active state) structures superimposed on the inactive CCR2 structure (CCR2-BMS681, PDB: 5T1A, green color). ( B ) Agonist-bound CCR8 (active state) structures superimposed on the inactive CCR5 structure (CCR5-maraviroc, PDB: 4MBS, yellow color). ( C to F ) Comparing the conformational changes in the conserved motif between activated CCR8 and inactive CCR2. The movement of F254 6.51 and the downward swing of W251 6.48 are indicated by red arrows. ( G to J ) Comparing the conformational changes in the conserved motif between activated CCR8 and inactive CCR5. LMD-009–bound CCR8 is shown in blue, and ZK 756326–bound CCR8 is shown in gray.

    Article Snippet: The codon-optimized nucleotide of WT CCR8 (UniProt ID P51685) was synthesized by GenScript.

    Techniques:

    ( A ) Overall comparison of three CCR8-G i structures by superposition on CCR8 (left); insertion of the α5-helix (G αi , cyan) into the CCR8 TMD represented as surface (right). ( B ) Molecular interactions between CCR8 and G αi shown in 2D. The interacting residues on G αi and CCR8 are shown in cyan and black, respectively. Residues on 7TM, ICL2, ICL3, and H8 are shown in light blue, pink, yellow, and cyan circles, respectively. Hydrogen bonds are highlighted with dashed red lines. ( C ) Sequence alignment of CCR1, CCR2, CCR3, CCR5, CCR6, and CCR8 in the regions of G protein interface. ( D and E ) Mutagenesis of G protein interface residues and functional measurement (G αβγ heterotrimer dissociation by BRET assay) of ZK 756326 (D)– or LMD-009 (E)–induced G i activation of CCR8. Data are means ± SEM.

    Journal: Science Advances

    Article Title: Unveiling the structural mechanisms of nonpeptide ligand recognition and activation in human chemokine receptor CCR8

    doi: 10.1126/sciadv.adj7500

    Figure Lengend Snippet: ( A ) Overall comparison of three CCR8-G i structures by superposition on CCR8 (left); insertion of the α5-helix (G αi , cyan) into the CCR8 TMD represented as surface (right). ( B ) Molecular interactions between CCR8 and G αi shown in 2D. The interacting residues on G αi and CCR8 are shown in cyan and black, respectively. Residues on 7TM, ICL2, ICL3, and H8 are shown in light blue, pink, yellow, and cyan circles, respectively. Hydrogen bonds are highlighted with dashed red lines. ( C ) Sequence alignment of CCR1, CCR2, CCR3, CCR5, CCR6, and CCR8 in the regions of G protein interface. ( D and E ) Mutagenesis of G protein interface residues and functional measurement (G αβγ heterotrimer dissociation by BRET assay) of ZK 756326 (D)– or LMD-009 (E)–induced G i activation of CCR8. Data are means ± SEM.

    Article Snippet: The codon-optimized nucleotide of WT CCR8 (UniProt ID P51685) was synthesized by GenScript.

    Techniques: Comparison, Sequencing, Mutagenesis, Functional Assay, Bioluminescence Resonance Energy Transfer, Activation Assay