Sandbox Reserved 430: Difference between revisions
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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> | 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> shown <scene name='48/483887/Binding/2'>here</scene>. 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. | ||
