7RQU
Cryo-EM structure of the full-length TRPV1 with RTx at 4 degrees Celsius, in a closed state, class I
Summary for 7RQU
| Entry DOI | 10.2210/pdb7rqu/pdb |
| EMDB information | 24636 |
| Descriptor | Transient receptor potential cation channel subfamily V member 1, resiniferatoxin, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine, ... (6 entities in total) |
| Functional Keywords | ligand-gating ion channel, membrane protein |
| Biological source | Rattus norvegicus (Rat) |
| Total number of polymer chains | 4 |
| Total formula weight | 420876.40 |
| Authors | |
| Primary citation | Kwon, D.H.,Zhang, F.,Fedor, J.G.,Suo, Y.,Lee, S.Y. Vanilloid-dependent TRPV1 opening trajectory from cryoEM ensemble analysis. Nat Commun, 13:2874-2874, 2022 Cited by PubMed Abstract: Single particle cryo-EM often yields multiple protein conformations within a single dataset, but experimentally deducing the temporal relationship of these conformers within a conformational trajectory is not trivial. Here, we use thermal titration methods and cryo-EM in an attempt to obtain temporal resolution of the conformational trajectory of the vanilloid receptor TRPV1 with resiniferatoxin (RTx) bound. Based on our cryo-EM ensemble analysis, RTx binding to TRPV1 appears to induce intracellular gate opening first, followed by selectivity filter dilation, then pore loop rearrangement to reach the final open state. This apparent conformational wave likely arises from the concerted, stepwise, additive structural changes of TRPV1 over many subdomains. Greater understanding of the RTx-mediated long-range allostery of TRPV1 could help further the therapeutic potential of RTx, which is a promising drug candidate for pain relief associated with advanced cancer or knee arthritis. PubMed: 35610228DOI: 10.1038/s41467-022-30602-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.05 Å) |
Structure validation
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