7MZ9
Cryo-EM structure of minimal TRPV1 with 1 partially bound RTX
Summary for 7MZ9
| Entry DOI | 10.2210/pdb7mz9/pdb |
| EMDB information | 24083 24084 24085 24086 24087 24088 24089 24090 24091 |
| Descriptor | Transient receptor potential cation channel subfamily V member 1, resiniferatoxin, (2S)-1-(butanoyloxy)-3-{[(R)-hydroxy{[(1r,2R,3S,4S,5R,6S)-2,3,4,5,6-pentahydroxycyclohexyl]oxy}phosphoryl]oxy}propan-2-yl tridecanoate, ... (4 entities in total) |
| Functional Keywords | trp channel, cryo-em, nanodisc, stoichiometry, transport protein |
| Biological source | Rattus norvegicus (Rat) |
| Total number of polymer chains | 4 |
| Total formula weight | 294519.00 |
| Authors | Zhang, K.,Julius, D.,Cheng, Y. (deposition date: 2021-05-24, release date: 2021-09-22, Last modification date: 2024-10-23) |
| Primary citation | Zhang, K.,Julius, D.,Cheng, Y. Structural snapshots of TRPV1 reveal mechanism of polymodal functionality. Cell, 184:5138-, 2021 Cited by PubMed Abstract: Many transient receptor potential (TRP) channels respond to diverse stimuli and conditionally conduct small and large cations. Such functional plasticity is presumably enabled by a uniquely dynamic ion selectivity filter that is regulated by physiological agents. What is currently missing is a "photo series" of intermediate structural states that directly address this hypothesis and reveal specific mechanisms behind such dynamic channel regulation. Here, we exploit cryoelectron microscopy (cryo-EM) to visualize conformational transitions of the capsaicin receptor, TRPV1, as a model to understand how dynamic transitions of the selectivity filter in response to algogenic agents, including protons, vanilloid agonists, and peptide toxins, permit permeation by small and large organic cations. These structures also reveal mechanisms governing ligand binding substates, as well as allosteric coupling between key sites that are proximal to the selectivity filter and cytoplasmic gate. These insights suggest a general framework for understanding how TRP channels function as polymodal signal integrators. PubMed: 34496225DOI: 10.1016/j.cell.2021.08.012 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.18 Å) |
Structure validation
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