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-Structure paper
タイトル | Extracellular cap domain is an essential component of the TRPV1 gating mechanism. |
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ジャーナル・号・ページ | Nat Commun, Vol. 12, Issue 1, Page 2154, Year 2021 |
掲載日 | 2021年4月12日 |
![]() | Kirill D Nadezhdin / Arthur Neuberger / Yury A Nikolaev / Lyle A Murphy / Elena O Gracheva / Sviatoslav N Bagriantsev / Alexander I Sobolevsky / ![]() |
PubMed 要旨 | Transient receptor potential (TRP) channels are polymodal molecular sensors involved in numerous physiological processes and implicated in a variety of human diseases. Several structures of the ...Transient receptor potential (TRP) channels are polymodal molecular sensors involved in numerous physiological processes and implicated in a variety of human diseases. Several structures of the founding member of the TRP channel family, TRPV1, are available, all of which were determined for the protein missing the N- and C-termini and the extracellular S5-P-loop. Here, we present structures of the full-length thirteen-lined ground squirrel TRPV1 solved by cryo-EM. Our structures resolve the extracellular cap domain formed by the S5-P-loops and the C-terminus that wraps around the three-stranded β-sheet connecting elements of the TRPV1 intracellular skirt. The cap domain forms a dome above the pore's extracellular entrance, with four portals leading to the ion conductance pathway. Deletion of the cap increases the TRPV1 average conductance, reduces the open probability and affects ion selectivity. Our data show that both the termini and the cap domain are critical determinants of TRPV1 function. |
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手法 | EM (単粒子) |
解像度 | 3.19 - 3.81 Å |
構造データ | EMDB-23491, PDB-7lqy: EMDB-23492, PDB-7lqz: EMDB-23493, PDB-7lr0: |
化合物 | ![]() ChemComp-POV: ![]() ChemComp-YBG: ![]() ChemComp-CL: ![]() ChemComp-NA: ![]() ChemComp-6EU: ![]() ChemComp-4DY: |
由来 |
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![]() | MEMBRANE PROTEIN / Transient Receptor Potential V Family Member 1 / TRP channel / TRPV1 full length / TRPV1 wild type / RTX / resiniferatoxin / capsaicin |