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. 2015 Dec 30;113(2):E137–E145. doi: 10.1073/pnas.1517288113

Fig. S2.

Fig. S2.

The vanilloid pocket of the apo protein (cyan, A), the TRPV1–CAPS complex (yellow, B), and the TRPV1–RTX complex (pink, C). (A) Tyr511 is oriented downward in the apo and upward in the protein–ligand complex structures. In the apo structure, the pocket is wide in all directions, facilitating ligand to get in. Tyr511 and Arg557 are oriented in such a way allowing pocket extension. Leu573 and Leu577 are oriented away from each other, leading to a wide subpocket in this direction. This wide pocket does not support tight ligand binding. (B) In the TRPV1–CAPS complex, the pocket is smaller in size compared with the one of the apo protein due to the upward orientation of Tyr511. A small volume is observed between Met547, Asn551, and Leu515. The bulk of the cavity is close to Tyr511 to accommodate the vanillyl group of CAPS and leading to hydrophobic contacts with between with Tyr511. (C) In the TRPV1–RTX complex, the pocket volume is smaller than the one of the apo protein due to upward orientation of Tyr511. Tyr511 and Glu570 are very close in TRPV1–RTX (∼2 Å apart). A wide volume is observed between Ala665, Leu669, and Leu674 and a small volume between Met547, Asn551, and Leu515. The bulk of the cavity is close to Leu669 to accommodate the large diterpene group of RTX.