Sandbox Reserved 430: Difference between revisions

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P2Y12R contains only one disulfide bond that connects the amino terminus with helix VII shown <scene name='48/483887/4ntj_disulfide_bond/1'>here</scene>. There are also two cholesterol molecules that are bound to two receptor molecules. One is bound between helix III and helix V and the other bound between helix I and helix VII.

P2Y12R contains only one disulfide bond that connects the amino terminus with helix VII shown <scene name='48/483887/4ntj_disulfide_bond/1'>here</scene>. There are also two cholesterol molecules that are bound to two receptor molecules. One is bound between helix III and helix V and the other bound between helix I and helix VII.

P2Y12R has some distinctive features from other GPCR structures in its family. Helix V, for example, has around two more helical turns and does not have the typical helical bend that other GPCR structures have. As mentioned above, helix V is <scene name='48/483887/Helix_vii/1'>elongated and straightened</scene>because the structure lacks proline and glycine residues to destabilize its structure. Furthermore, the elongated and straightened conformation causes P2Y12R’s extracellular end to shift 6 Å closer to helix IV compared to other class A GPCR structures. In addition, the intracellular tip of helix VII is closer to the seven transmembrane helical bundle. Helix VI’s intracellular tip is tilted slightly outward and shifted closer to the intracellular surface than other GPCR structures.

P2Y12R has some distinctive features from other GPCR structures in its family. Helix V, for example, has around two more helical turns and does not have the typical helical bend that other GPCR structures have. As mentioned above, helix V is <scene name='48/483887/Helix_vii/1'>elongated and straightened</scene> because the structure lacks proline and glycine residues to destabilize its structure. Furthermore, the elongated and straightened conformation causes P2Y12R’s extracellular end to shift 6 Å closer to helix IV compared to other class A GPCR structures. In addition, the intracellular tip of helix VII is closer to the seven transmembrane helical bundle. Helix VI’s intracellular tip is tilted slightly outward and shifted closer to the intracellular surface than other GPCR structures.

This <scene name='48/483887/Polar__nonpolar/1'>view</scene> demonstrates the polar and nonpolar regions of the P2Y12R's structure. AZD1283 spans more than 17 Å between helix IV and helix VII contributing to the polar and hydrophobic bonding with helices III–VI.

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 {{Template:ColorKey_N2CRainbow}}
-P2Y12R contains only one <font color='yellow'>disulfide bond</font> that connects the <font color='blue'>amino terminus</font> with <font color='darkorgange'>helix VII</font> shown <scene name='48/483887/4ntj_disulfide_bond/1'>here</scene>. There are also two cholesterol molecules that are bound to two receptor molecules. One is bound between <font color='deepbluesky'>helix III</font> and <font color='lime>helix V</font> and the other bound between <font color='blue'>helix I</font> and <font color='darkorange'>helix VII</font>.
+P2Y12R contains only one <font color='gold'>disulfide bond</font> that connects the <font color='blue'>amino terminus</font> with <font color='darkorgange'>helix VII</font> shown <scene name='48/483887/4ntj_disulfide_bond/1'>here</scene>. There are also two cholesterol molecules that are bound to two receptor molecules. One is bound between <font color='deepbluesky'>helix III</font> and <font color='lime>helix V</font> and the other bound between <font color='blue'>helix I</font> and <font color='darkorange'>helix VII</font>.
-P2Y12R has some distinctive features from other GPCR structures in its family. <font color='lime'>Helix V</font>, for example, has around two more helical turns and does not have the typical helical bend that other GPCR structures have. As mentioned above, <font color='lime'>helix V</font> is <scene name='48/483887/Helix_vii/1'>elongated and straightened</scene>because the structure lacks proline and glycine residues to destabilize its structure. Furthermore, the elongated and straightened conformation causes P2Y12R’s extracellular end to shift 6 Å closer to <font color='turquoise'>helix IV</font> compared to other class A GPCR structures. In addition, the intracellular tip of <font color='darkorange'>helix VII</font> is closer to the seven transmembrane helical bundle. <font color='gold'>Helix VI’s</font> intracellular tip is tilted slightly outward and shifted closer to the intracellular surface than other GPCR structures.
+P2Y12R has some distinctive features from other GPCR structures in its family. <font color='lime'>Helix V</font>, for example, has around two more helical turns and does not have the typical helical bend that other GPCR structures have. As mentioned above, <font color='lime'>helix V</font> is <scene name='48/483887/Helix_vii/1'>elongated and straightened</scene> because the structure lacks proline and glycine residues to destabilize its structure. Furthermore, the elongated and straightened conformation causes P2Y12R’s extracellular end to shift 6 Å closer to <font color='turquoise'>helix IV</font> compared to other class A GPCR structures. In addition, the intracellular tip of <font color='darkorange'>helix VII</font> is closer to the seven transmembrane helical bundle. <font color='gold'>Helix VI’s</font> intracellular tip is tilted slightly outward and shifted closer to the intracellular surface than other GPCR structures.
 This <scene name='48/483887/Polar__nonpolar/1'>view</scene> demonstrates the polar and nonpolar regions of the P2Y12R's structure. AZD1283 spans more than 17 Å between <font color='turquoise'>helix IV</font> and <font color='darkorange'>helix VII</font> contributing to the polar and hydrophobic bonding with helices III–VI.

Sandbox Reserved 430: Difference between revisions

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