trimeric p2x1 receptor (Danaher Inc)

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Danaher Inc trimeric p2x1 receptor

A) Cryo-EM map of the ATP-bound <t>P2X1</t> receptor, with chains coloured individually and the cryo-EM ligand density depicted in violet. An enlarged image of Mg-ATP and nearby water molecules was fitted into the cryo-EM map. B) Cryo-EM map of the NF449-bound P2X1 receptor, with chains coloured individually and the cryo-EM ligand density depicted in violet. An enlarged image of NF449 was fitted into the cryo-EM map. C) Structural characteristics of the monomer from the ATP-bound P2X1 receptor and the NF449-bound P2X1 receptor colourised to resemble features of a dolphin. The head domain is colored purple, the lower body is light blue, the dorsal fin is orange, the upper body is blue, the right flipper is red, the left flipper is yellow, and the fluke is green.

Trimeric P2x1 Receptor, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/trimeric p2x1 receptor/product/Danaher Inc
Average 86 stars, based on 1 article reviews
Price from $9.99 to $1999.99

trimeric p2x1 receptor - by Bioz Stars, 2024-09

86/100 stars

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1) Product Images from "Structural insights into the human P2X1 receptor and ligand interactions"

Article Title: Structural insights into the human P2X1 receptor and ligand interactions

Journal: bioRxiv

doi: 10.1101/2024.04.04.588192

A) Cryo-EM map of the ATP-bound P2X1 receptor, with chains coloured individually and the cryo-EM ligand density depicted in violet. An enlarged image of Mg-ATP and nearby water molecules was fitted into the cryo-EM map. B) Cryo-EM map of the NF449-bound P2X1 receptor, with chains coloured individually and the cryo-EM ligand density depicted in violet. An enlarged image of NF449 was fitted into the cryo-EM map. C) Structural characteristics of the monomer from the ATP-bound P2X1 receptor and the NF449-bound P2X1 receptor colourised to resemble features of a dolphin. The head domain is colored purple, the lower body is light blue, the dorsal fin is orange, the upper body is blue, the right flipper is red, the left flipper is yellow, and the fluke is green.

Figure Legend Snippet: A) Cryo-EM map of the ATP-bound P2X1 receptor, with chains coloured individually and the cryo-EM ligand density depicted in violet. An enlarged image of Mg-ATP and nearby water molecules was fitted into the cryo-EM map. B) Cryo-EM map of the NF449-bound P2X1 receptor, with chains coloured individually and the cryo-EM ligand density depicted in violet. An enlarged image of NF449 was fitted into the cryo-EM map. C) Structural characteristics of the monomer from the ATP-bound P2X1 receptor and the NF449-bound P2X1 receptor colourised to resemble features of a dolphin. The head domain is colored purple, the lower body is light blue, the dorsal fin is orange, the upper body is blue, the right flipper is red, the left flipper is yellow, and the fluke is green.

Techniques Used: Cryo-EM Sample Prep

Cartoon representation of the A) ATP-bound P2X1 receptor and B) NF449-bound P2X1 receptor coloured by monomer. The surface volume of the pore radius is highlighted in red, white, and blue, with red indicating the area with the tightest constriction point. C) Graph of the pore radius along the length of the pore region with the residues responsible for constricting the pore radii highlighted. The ATP-bound P2X1 receptor is depicted in blue, while the NF449-bound P2X1 receptor is represented in red. The pore radius measured 0.6 Å for the ATP-bound receptor and 1.0 Å for the NF449-bound receptor, indicated by the dotted line. D) Transmembrane domains of the ATP-bound P2X1 receptor (red) are overlaid with those of the ATP-bound hP2X3 receptor (5SVL, green). Additionally, transmembrane domains of the NF449-bound P2X1 receptor (blue) are overlaid with those of the TNP-ATP-bound hP2X3 receptor (5SVQ, yellow).

Figure Legend Snippet: Cartoon representation of the A) ATP-bound P2X1 receptor and B) NF449-bound P2X1 receptor coloured by monomer. The surface volume of the pore radius is highlighted in red, white, and blue, with red indicating the area with the tightest constriction point. C) Graph of the pore radius along the length of the pore region with the residues responsible for constricting the pore radii highlighted. The ATP-bound P2X1 receptor is depicted in blue, while the NF449-bound P2X1 receptor is represented in red. The pore radius measured 0.6 Å for the ATP-bound receptor and 1.0 Å for the NF449-bound receptor, indicated by the dotted line. D) Transmembrane domains of the ATP-bound P2X1 receptor (red) are overlaid with those of the ATP-bound hP2X3 receptor (5SVL, green). Additionally, transmembrane domains of the NF449-bound P2X1 receptor (blue) are overlaid with those of the TNP-ATP-bound hP2X3 receptor (5SVQ, yellow).

Techniques Used:

A) Overlay of the ATP-bound P2X1 receptor (red) and NF449-bound P2X1 receptor (blue) at the orthosteric binding site, illustrating movement in secondary structure with arrows. B) Overlay of the ATP-bound P2X1 receptor (red) and NF449-bound P2X1 receptor (blue) at the lower body and transmembrane domain, illustrating movement in secondary structure with arrows.

Figure Legend Snippet: A) Overlay of the ATP-bound P2X1 receptor (red) and NF449-bound P2X1 receptor (blue) at the orthosteric binding site, illustrating movement in secondary structure with arrows. B) Overlay of the ATP-bound P2X1 receptor (red) and NF449-bound P2X1 receptor (blue) at the lower body and transmembrane domain, illustrating movement in secondary structure with arrows.

Techniques Used: Binding Assay

Calculated EC50 values of α,β-methylene ATP derived from pooled data of four individual

Figure Legend Snippet:

Techniques Used: Derivative Assay, Expressing, Residue

A) Depiction of the ATP binding site where the key interactions are illustrated as black dotted lines, accompanied by labeling of nearby residues. B, C) Increasing concentrations of the agonist α,β-methylene ATP on HEK293 cells expressing WT-P2X1 or single residue mutants of the P2X1 receptor. The data is normalized to 10 µM ionomycin and subsequently adjusted so that the highest value corresponds to 100 and the lowest value to 0. It is then fitted to a log(agonist) nonlinear regression curve using a four-parameter model, with the top and bottom constrained to 100 and 0, respectively. Results are presented as mean ± SEM, with n = 4 replicates. The left graph contains mutants designed for the ATP-bound P2X1 receptor and the right graph contains mutants designed for the NF449-bound P2X1 receptor. D) Amino acid sequence alignment of key residues from the human P2X1 receptor (hP2X1:P51575), aligned with corresponding residues from other human P2X receptor subtypes (hP2X2:Q9UBL9, hP2X3:P56373, hP2X4:Q99571, hP2X5:Q93086, hP2X6:O15547, hP2X7:Q99572). Residue categorisation based on properties: Hydrophobic (A, I, L, M, F, W, V, Y) in blue, positive charge (K, R, H) in red, negative charge (E, D) in magenta, polar (N, Q, S, T) in green. Special cases (C, G, P) in orange. Gaps are represented in white.

Figure Legend Snippet: A) Depiction of the ATP binding site where the key interactions are illustrated as black dotted lines, accompanied by labeling of nearby residues. B, C) Increasing concentrations of the agonist α,β-methylene ATP on HEK293 cells expressing WT-P2X1 or single residue mutants of the P2X1 receptor. The data is normalized to 10 µM ionomycin and subsequently adjusted so that the highest value corresponds to 100 and the lowest value to 0. It is then fitted to a log(agonist) nonlinear regression curve using a four-parameter model, with the top and bottom constrained to 100 and 0, respectively. Results are presented as mean ± SEM, with n = 4 replicates. The left graph contains mutants designed for the ATP-bound P2X1 receptor and the right graph contains mutants designed for the NF449-bound P2X1 receptor. D) Amino acid sequence alignment of key residues from the human P2X1 receptor (hP2X1:P51575), aligned with corresponding residues from other human P2X receptor subtypes (hP2X2:Q9UBL9, hP2X3:P56373, hP2X4:Q99571, hP2X5:Q93086, hP2X6:O15547, hP2X7:Q99572). Residue categorisation based on properties: Hydrophobic (A, I, L, M, F, W, V, Y) in blue, positive charge (K, R, H) in red, negative charge (E, D) in magenta, polar (N, Q, S, T) in green. Special cases (C, G, P) in orange. Gaps are represented in white.

Techniques Used: Binding Assay, Labeling, Expressing, Residue, Sequencing

Calculated IC50 values of NF449 derived from pooled data of three to four

Figure Legend Snippet:

Techniques Used: Derivative Assay, Expressing, Residue

A) Depiction of the NF449 binding site where the key interactions are illustrated as black dotted lines, accompanied by labelling of nearby residues. B, C) Submaximal concentrations of α,β-methylene ATP (0.316 - 100 µM, 80-95% of max per mutant) with increasing concentrations of the antagonist NF449 on HEK293 cells expressing WT-P2X1 and single residue mutants of the P2X1 receptor. The data is normalized to 10 µM ionomycin and subsequently adjusted so that the highest value corresponds to 100 and the lowest value to 0. It is then fitted to a log(antagonist) nonlinear regression curve fit (four parameters) with the top and bottom constrained to 100 and 0, respectively. Results are presented as mean ± SEM, with n = 3 - 4 replicates. The left graph contains data for single alanine mutants, and the right graph contains data for P2X1 to P2X7 single residue mutants. D) Amino acid sequence alignment of key residues from the human P2X1 receptor (hP2X1:P51575), aligned with corresponding residues from other human P2X receptor subtypes (hP2X2:Q9UBL9, hP2X3:P56373, hP2X4:Q99571, hP2X5:Q93086, hP2X6:O15547, hP2X7:Q99572). Residue categorisation based on properties: Hydrophobic (A, I, L, M, F, W, V, Y) in blue, positive charge (K, R, H) in red, negative charge (E, D) in magenta, polar (N, Q, S, T) in green. Special cases (C, G, P) in orange. Gaps are represented in white.

Figure Legend Snippet: A) Depiction of the NF449 binding site where the key interactions are illustrated as black dotted lines, accompanied by labelling of nearby residues. B, C) Submaximal concentrations of α,β-methylene ATP (0.316 - 100 µM, 80-95% of max per mutant) with increasing concentrations of the antagonist NF449 on HEK293 cells expressing WT-P2X1 and single residue mutants of the P2X1 receptor. The data is normalized to 10 µM ionomycin and subsequently adjusted so that the highest value corresponds to 100 and the lowest value to 0. It is then fitted to a log(antagonist) nonlinear regression curve fit (four parameters) with the top and bottom constrained to 100 and 0, respectively. Results are presented as mean ± SEM, with n = 3 - 4 replicates. The left graph contains data for single alanine mutants, and the right graph contains data for P2X1 to P2X7 single residue mutants. D) Amino acid sequence alignment of key residues from the human P2X1 receptor (hP2X1:P51575), aligned with corresponding residues from other human P2X receptor subtypes (hP2X2:Q9UBL9, hP2X3:P56373, hP2X4:Q99571, hP2X5:Q93086, hP2X6:O15547, hP2X7:Q99572). Residue categorisation based on properties: Hydrophobic (A, I, L, M, F, W, V, Y) in blue, positive charge (K, R, H) in red, negative charge (E, D) in magenta, polar (N, Q, S, T) in green. Special cases (C, G, P) in orange. Gaps are represented in white.

Techniques Used: Binding Assay, Mutagenesis, Expressing, Residue, Sequencing

Magnified image of the ATP binding site at the P2X1, hP2X3 (5SVL), zfP2X4 (4DW1), and rP2X7 (6U9W) receptor structures where the key interactions are illustrated as black dotted lines, accompanied by labelling of nearby residues. RMSD of ATP in the P2X1 receptor compared to bound ATP in the hP2X3, zfP2X4, and rP2X7 receptors: 0.70, 0.93, and 1.3, respectively.

Figure Legend Snippet: Magnified image of the ATP binding site at the P2X1, hP2X3 (5SVL), zfP2X4 (4DW1), and rP2X7 (6U9W) receptor structures where the key interactions are illustrated as black dotted lines, accompanied by labelling of nearby residues. RMSD of ATP in the P2X1 receptor compared to bound ATP in the hP2X3, zfP2X4, and rP2X7 receptors: 0.70, 0.93, and 1.3, respectively.

Techniques Used: Binding Assay

Overlay of the NF449 binding site from the P2X1 receptor structure (blue) compared to A-317491 from the hP2X3 receptor (5SVR, violet), PPNDS from the pdP2X4 receptor (8JV8, green), and TNP-ATP from the ckP2X7 receptor (5XW6, yellow). The 2D chemical structures for each of these ligands are depicted.

Figure Legend Snippet: Overlay of the NF449 binding site from the P2X1 receptor structure (blue) compared to A-317491 from the hP2X3 receptor (5SVR, violet), PPNDS from the pdP2X4 receptor (8JV8, green), and TNP-ATP from the ckP2X7 receptor (5XW6, yellow). The 2D chemical structures for each of these ligands are depicted.

Techniques Used: Binding Assay

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trimeric p2x1 receptor (Danaher Inc)

Danaher Inc trimeric p2x1 receptor

trimeric p2x1 receptor - by Bioz Stars, 2024-09

86/100 stars

Buy from Supplier

Image Search Results

Journal: bioRxiv

Article Title: Structural insights into the human P2X1 receptor and ligand interactions

doi: 10.1101/2024.04.04.588192

Figure Lengend Snippet: A) Cryo-EM map of the ATP-bound P2X1 receptor, with chains coloured individually and the cryo-EM ligand density depicted in violet. An enlarged image of Mg-ATP and nearby water molecules was fitted into the cryo-EM map. B) Cryo-EM map of the NF449-bound P2X1 receptor, with chains coloured individually and the cryo-EM ligand density depicted in violet. An enlarged image of NF449 was fitted into the cryo-EM map. C) Structural characteristics of the monomer from the ATP-bound P2X1 receptor and the NF449-bound P2X1 receptor colourised to resemble features of a dolphin. The head domain is colored purple, the lower body is light blue, the dorsal fin is orange, the upper body is blue, the right flipper is red, the left flipper is yellow, and the fluke is green.

Article Snippet: The sample was loaded onto a pre-equilibrated Superdex 200 Increase 10/300 GL column (Cytiva, USA), and fractions containing the trimeric P2X1 receptor were pooled, concentrated, flash-frozen in liquid nitrogen, and stored at −80⁰C.

Techniques: Cryo-EM Sample Prep

Journal: bioRxiv

Article Title: Structural insights into the human P2X1 receptor and ligand interactions

doi: 10.1101/2024.04.04.588192

Figure Lengend Snippet: Cartoon representation of the A) ATP-bound P2X1 receptor and B) NF449-bound P2X1 receptor coloured by monomer. The surface volume of the pore radius is highlighted in red, white, and blue, with red indicating the area with the tightest constriction point. C) Graph of the pore radius along the length of the pore region with the residues responsible for constricting the pore radii highlighted. The ATP-bound P2X1 receptor is depicted in blue, while the NF449-bound P2X1 receptor is represented in red. The pore radius measured 0.6 Å for the ATP-bound receptor and 1.0 Å for the NF449-bound receptor, indicated by the dotted line. D) Transmembrane domains of the ATP-bound P2X1 receptor (red) are overlaid with those of the ATP-bound hP2X3 receptor (5SVL, green). Additionally, transmembrane domains of the NF449-bound P2X1 receptor (blue) are overlaid with those of the TNP-ATP-bound hP2X3 receptor (5SVQ, yellow).

Techniques:

Journal: bioRxiv

Article Title: Structural insights into the human P2X1 receptor and ligand interactions

doi: 10.1101/2024.04.04.588192

Figure Lengend Snippet: A) Overlay of the ATP-bound P2X1 receptor (red) and NF449-bound P2X1 receptor (blue) at the orthosteric binding site, illustrating movement in secondary structure with arrows. B) Overlay of the ATP-bound P2X1 receptor (red) and NF449-bound P2X1 receptor (blue) at the lower body and transmembrane domain, illustrating movement in secondary structure with arrows.

Techniques: Binding Assay

Journal: bioRxiv

Article Title: Structural insights into the human P2X1 receptor and ligand interactions

doi: 10.1101/2024.04.04.588192

Figure Lengend Snippet:

Techniques: Derivative Assay, Expressing, Residue

Journal: bioRxiv

Article Title: Structural insights into the human P2X1 receptor and ligand interactions

doi: 10.1101/2024.04.04.588192

Figure Lengend Snippet: A) Depiction of the ATP binding site where the key interactions are illustrated as black dotted lines, accompanied by labeling of nearby residues. B, C) Increasing concentrations of the agonist α,β-methylene ATP on HEK293 cells expressing WT-P2X1 or single residue mutants of the P2X1 receptor. The data is normalized to 10 µM ionomycin and subsequently adjusted so that the highest value corresponds to 100 and the lowest value to 0. It is then fitted to a log(agonist) nonlinear regression curve using a four-parameter model, with the top and bottom constrained to 100 and 0, respectively. Results are presented as mean ± SEM, with n = 4 replicates. The left graph contains mutants designed for the ATP-bound P2X1 receptor and the right graph contains mutants designed for the NF449-bound P2X1 receptor. D) Amino acid sequence alignment of key residues from the human P2X1 receptor (hP2X1:P51575), aligned with corresponding residues from other human P2X receptor subtypes (hP2X2:Q9UBL9, hP2X3:P56373, hP2X4:Q99571, hP2X5:Q93086, hP2X6:O15547, hP2X7:Q99572). Residue categorisation based on properties: Hydrophobic (A, I, L, M, F, W, V, Y) in blue, positive charge (K, R, H) in red, negative charge (E, D) in magenta, polar (N, Q, S, T) in green. Special cases (C, G, P) in orange. Gaps are represented in white.

Techniques: Binding Assay, Labeling, Expressing, Residue, Sequencing

Journal: bioRxiv

Article Title: Structural insights into the human P2X1 receptor and ligand interactions

doi: 10.1101/2024.04.04.588192

Figure Lengend Snippet: A) Depiction of the NF449 binding site where the key interactions are illustrated as black dotted lines, accompanied by labelling of nearby residues. B, C) Submaximal concentrations of α,β-methylene ATP (0.316 - 100 µM, 80-95% of max per mutant) with increasing concentrations of the antagonist NF449 on HEK293 cells expressing WT-P2X1 and single residue mutants of the P2X1 receptor. The data is normalized to 10 µM ionomycin and subsequently adjusted so that the highest value corresponds to 100 and the lowest value to 0. It is then fitted to a log(antagonist) nonlinear regression curve fit (four parameters) with the top and bottom constrained to 100 and 0, respectively. Results are presented as mean ± SEM, with n = 3 - 4 replicates. The left graph contains data for single alanine mutants, and the right graph contains data for P2X1 to P2X7 single residue mutants. D) Amino acid sequence alignment of key residues from the human P2X1 receptor (hP2X1:P51575), aligned with corresponding residues from other human P2X receptor subtypes (hP2X2:Q9UBL9, hP2X3:P56373, hP2X4:Q99571, hP2X5:Q93086, hP2X6:O15547, hP2X7:Q99572). Residue categorisation based on properties: Hydrophobic (A, I, L, M, F, W, V, Y) in blue, positive charge (K, R, H) in red, negative charge (E, D) in magenta, polar (N, Q, S, T) in green. Special cases (C, G, P) in orange. Gaps are represented in white.

Techniques: Binding Assay, Mutagenesis, Expressing, Residue, Sequencing

Journal: bioRxiv

Article Title: Structural insights into the human P2X1 receptor and ligand interactions

doi: 10.1101/2024.04.04.588192

Figure Lengend Snippet: Magnified image of the ATP binding site at the P2X1, hP2X3 (5SVL), zfP2X4 (4DW1), and rP2X7 (6U9W) receptor structures where the key interactions are illustrated as black dotted lines, accompanied by labelling of nearby residues. RMSD of ATP in the P2X1 receptor compared to bound ATP in the hP2X3, zfP2X4, and rP2X7 receptors: 0.70, 0.93, and 1.3, respectively.

Techniques: Binding Assay

Journal: bioRxiv

Article Title: Structural insights into the human P2X1 receptor and ligand interactions

doi: 10.1101/2024.04.04.588192

Figure Lengend Snippet: Overlay of the NF449 binding site from the P2X1 receptor structure (blue) compared to A-317491 from the hP2X3 receptor (5SVR, violet), PPNDS from the pdP2X4 receptor (8JV8, green), and TNP-ATP from the ckP2X7 receptor (5XW6, yellow). The 2D chemical structures for each of these ligands are depicted.

Techniques: Binding Assay