5AN8
Cryo-electron microscopy structure of rabbit TRPV2 ion channel
Summary for 5AN8
| Entry DOI | 10.2210/pdb5an8/pdb |
| EMDB information | 6455 |
| Descriptor | TRPV2 (1 entity in total) |
| Functional Keywords | transport protein, trp channel |
| Biological source | ORYCTOLAGUS CUNICULUS (RABBIT) |
| Total number of polymer chains | 4 |
| Total formula weight | 279625.56 |
| Authors | Zubcevic, L.,Herzik, M.A.J.,Chung, B.C.,Lander, G.C.,Lee, S.Y. (deposition date: 2015-09-04, release date: 2015-12-23, Last modification date: 2024-10-16) |
| Primary citation | Zubcevic, L.,Herzik, M.,Chung, B.C.,Lander, G.C.,Lee, S.Y. Cryo-Electron Microscopy of the Trpv2 Ion Channel Nat.Struct.Mol.Biol., 23:180-, 2016 Cited by PubMed Abstract: Transient receptor potential vanilloid (TRPV) cation channels are polymodal sensors involved in a variety of physiological processes. TRPV2, a member of the TRPV family, is regulated by temperature, by ligands, such as probenecid and cannabinoids, and by lipids. TRPV2 has been implicated in many biological functions, including somatosensation, osmosensation and innate immunity. Here we present the atomic model of rabbit TRPV2 in its putative desensitized state, as determined by cryo-EM at a nominal resolution of ∼4 Å. In the TRPV2 structure, the transmembrane segment 6 (S6), which is involved in gate opening, adopts a conformation different from the one observed in TRPV1. Structural comparisons of TRPV1 and TRPV2 indicate that a rotation of the ankyrin-repeat domain is coupled to pore opening via the TRP domain, and this pore opening can be modulated by rearrangements in the secondary structure of S6. PubMed: 26779611DOI: 10.1038/NSMB.3159 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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