6bbj | pdb_00006bbj

Xenopus Tropicalis TRPV4

spinqualitylabelsall models 6bbj, resolution 3.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6bbj is a 4 chain structure with sequence from Silurana (xenopus) tropicalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: trpv4 (Silurana (Xenopus) tropicalis) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The transient receptor potential (TRP) channel TRPV4 participates in multiple biological processes, and numerous TRPV4 mutations underlie several distinct and devastating diseases. Here we present the cryo-EM structure of Xenopus tropicalis TRPV4 at 3.8-A resolution. The ion-conduction pore contains an intracellular gate formed by the inner helices, but lacks any extracellular gate in the selectivity filter, as observed in other TRPV channels. Anomalous X-ray diffraction analyses identify a single ion-binding site in the selectivity filter, thus explaining TRPV4 nonselectivity. Structural comparisons with other TRP channels and distantly related voltage-gated cation channels reveal an unprecedented, unique packing interface between the voltage-sensor-like domain and the pore domain, suggesting distinct gating mechanisms. Moreover, our structure begins to provide mechanistic insights to the large set of pathogenic mutations, offering potential opportunities for drug development. Cryo-EM and X-ray structures of TRPV4 reveal insight into ion permeation and gating mechanisms.,Deng Z, Paknejad N, Maksaev G, Sala-Rabanal M, Nichols CG, Hite RK, Yuan P Nat Struct Mol Biol. 2018 Mar;25(3):252-260. doi: 10.1038/s41594-018-0037-5. Epub, 2018 Feb 26. PMID:29483651 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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