6OT2
Structure of the TRPV3 K169A sensitized mutant in apo form at 4.1 A resolution
Summary for 6OT2
| Entry DOI | 10.2210/pdb6ot2/pdb |
| EMDB information | 20192 20194 |
| Descriptor | Transient receptor potential cation channel subfamily V member 3 (1 entity in total) |
| Functional Keywords | ion channel, trp channel, trpv channel, metal transport, membrane transport, membrane protein, transport protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 337781.91 |
| Authors | Zubcevic, L.,Borschel, W.F.,Hsu, A.L.,Borgnia, M.J.,Lee, S.-Y. (deposition date: 2019-05-02, release date: 2019-05-22, Last modification date: 2024-03-20) |
| Primary citation | Zubcevic, L.,Borschel, W.F.,Hsu, A.L.,Borgnia, M.J.,Lee, S.Y. Regulatory switch at the cytoplasmic interface controls TRPV channel gating. Elife, 8:-, 2019 Cited by PubMed Abstract: Temperature-sensitive transient receptor potential vanilloid (thermoTRPV) channels are activated by ligands and heat, and are involved in various physiological processes. ThermoTRPV channels possess a large cytoplasmic ring consisting of N-terminal ankyrin repeat domains (ARD) and C-terminal domains (CTD). The cytoplasmic inter-protomer interface is unique and consists of a CTD coiled around a β-sheet which makes contacts with the neighboring ARD. Despite much existing evidence that the cytoplasmic ring is important for thermoTRPV function, the mechanism by which this unique structure is involved in thermoTRPV gating has not been clear. Here, we present cryo-EM and electrophysiological studies which demonstrate that TRPV3 gating involves large rearrangements at the cytoplasmic inter-protomer interface and that this motion triggers coupling between cytoplasmic and transmembrane domains, priming the channel for opening. Furthermore, our studies unveil the role of this interface in the distinct biophysical and physiological properties of individual thermoTRPV subtypes. PubMed: 31070581DOI: 10.7554/eLife.47746 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.1 Å) |
Structure validation
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