Sandbox Reserved 430: Difference between revisions

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==Overall Structure==

The <scene name='48/483887/Secondary_structure/2'>secondary structure</scene> consists of eight alpha helices. The overall fold has seven transmembrane alpha helices and a carboxy-terminal helix VII, which is parallel to the membrane bilayer. There is only one disulphide bond found in its structure that connects the amino terminus (C17) with helix VII. Two cholesterol molecules are bound to two receptor molecules.

The <scene name='48/483887/Secondary_structure/2'>secondary structure</scene> consists of eight alpha helices. The overall fold has seven transmembrane alpha helices and a carboxy-terminal helix VII, which is parallel to the membrane bilayer. There is only one disulphide bond found in its structure that connects the amino terminus (C17) with helix VII. Two cholesterol molecules are bound to two receptor molecules.

P2Y12R has some distinctive features. Helix V, for example, has ~2 more helical turns does not have the helical bend that other GPCR structures have. As mentioned above, helix V is <scene name='48/483887/Elongated_and_straightened/3'>elongated and straightened</scene> because the structure lacks proline and glycine residues to destabilize its structure. Compared to other GPCR structures, the intracellular tip of helix VII is of helix VII is closer to the seven transmembrane helical bundle. The intracellular tip of helix VI is shifted slightly outward.

Sandbox Reserved 430: Difference between revisions

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@@ Line 19: / Line 19: @@
 ==Overall Structure==
-The <scene name='48/483887/Secondary_structure/2'>secondary structure</scene> consists of eight <font color='deeppink'> alpha helices</font>. The overall fold has seven transmembrane alpha helices and a carboxy-terminal helix VII, which is parallel to the membrane bilayer. There is only one disulphide bond found in its structure that connects the amino terminus (C17) with helix VII. Two <font color='blue'> cholesterol molecules </font> are  bound to two <font color='blue'> receptor molecules</font>.
+The <scene name='48/483887/Secondary_structure/2'>secondary structure</scene> consists of eight <font color='deeppink'> alpha helices</font>. The overall fold has seven transmembrane alpha helices and a carboxy-terminal helix VII, which is parallel to the membrane bilayer. There is only one <font color='purple'>disulphide bond</font> found in its structure that connects the amino terminus (C17) with helix VII. Two <font color='blue'> cholesterol molecules </font> are  bound to two <font color='blue'> receptor molecules</font>.
 P2Y12R has some distinctive features. Helix V, for example, has ~2 more helical turns does not have the helical bend that other GPCR structures have. As mentioned above, helix V is <scene name='48/483887/Elongated_and_straightened/3'>elongated and straightened</scene> because the structure lacks proline and glycine residues to destabilize its structure. Compared to other GPCR structures, the intracellular tip of helix VII is of helix VII is closer to the seven transmembrane helical bundle. The intracellular tip of helix VI is shifted slightly outward.