Sandbox Reserved 1652: Difference between revisions
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Stimulation by resiniferatoxin makes this ion channel permeable to cations, especially calcium. | Stimulation by resiniferatoxin makes this ion channel permeable to cations, especially calcium. | ||
The pocket size characteristics of the TRPV1-RTX allow the installation of large structures such as the RTX : The '''sub-pocket''' near Y511 is shallow in the TRPV1-RTX because Y511 and E570 are close and I569 is oriented towards the vanilloid pocket. | The pocket size characteristics of the TRPV1-RTX allow the installation of large structures such as the RTX : The '''sub-pocket''' near <scene name='86/868185/Y511/2'>Y511</scene> is shallow in the TRPV1-RTX because <scene name='86/868185/Y511/2'>Y511</scene> and E570 are close and I569 is oriented towards the vanilloid pocket. | ||
The sub-pocket near L669, V583, and F587 is wide due to the projection of these amino acids out of the vanilloid pocket. This sub-pocket accommodates the [https://en.wikipedia.org/wiki/Diterpene diterpene] group of the RTX. | The sub-pocket near L669, V583, and F587 is wide due to the projection of these amino acids out of the vanilloid pocket. This sub-pocket accommodates the [https://en.wikipedia.org/wiki/Diterpene diterpene] group of the RTX. | ||
However, the orientation of L515 and M547 makes this region of the vanilloid pocket narrow, which considerably limits the nature of the fragments tolerated. | However, the orientation of L515 and M547 makes this region of the vanilloid pocket narrow, which considerably limits the nature of the fragments tolerated. | ||
The aromatic part of resiniferatoxin is located deeper in the sub-pocket near Y511 and is oriented almost parallel to the aromatic side chain of Y511, so it establishes a strong interaction π-π. The aromatic hydroxyl and methoxy groups of the RTX form strong hydrogen bonds with E570, R557 and S512. The ester group is linked to Y511 and T550 by hydrogen bonds.<ref>K. Elokely et al., « Understanding TRPV1 activation by ligands: Insights from the binding modes of capsaicin and resiniferatoxin », Proc. Natl. Acad. Sci., vol. 113, no 2, p. E137‑E145, janv. 2016, doi:10.1073/pnas.1517288113.</ref> | The aromatic part of resiniferatoxin is located deeper in the sub-pocket near <scene name='86/868185/Y511/2'>Y511</scene> and is oriented almost parallel to the aromatic side chain of <scene name='86/868185/Y511/2'>Y511</scene>, so it establishes a strong interaction π-π. The aromatic hydroxyl and methoxy groups of the RTX form strong hydrogen bonds with E570, R557 and S512. The ester group is linked to <scene name='86/868185/Y511/2'>Y511</scene> and T550 by hydrogen bonds.<ref>K. Elokely et al., « Understanding TRPV1 activation by ligands: Insights from the binding modes of capsaicin and resiniferatoxin », Proc. Natl. Acad. Sci., vol. 113, no 2, p. E137‑E145, janv. 2016, doi:10.1073/pnas.1517288113.</ref> | ||
=== Regulation === | === Regulation === | ||
