6ot5 | pdb_00006ot5

Structure of the TRPV3 K169A sensitized mutant in the presence of 2-APB at 3.6 A resolution

spinqualitylabelsall models 6ot5, resolution 3.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ot5 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FZ4 NonStd Res: UNK Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 b-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. Regulatory switch at the cytoplasmic interface controls TRPV channel gating.,Zubcevic L, Borschel WF, Hsu AL, Borgnia MJ, Lee SY Elife. 2019 May 9;8. pii: 47746. doi: 10.7554/eLife.47746. PMID:31070581 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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