6bwj

Crystal structure of the TRPV2 ion channel in complex with RTx

spinqualitylabelsall models 6bwj, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6bwj is a 2 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.1Å Ligands: 6EU, CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G1SNM3_RABIT Publication Abstract from PubMed Transient receptor potential vanilloid (TRPV) channels are activated by ligands and heat and are involved in various physiological processes. In contrast to the architecturally related voltage-gated cation channels, TRPV1 and TRPV2 subtypes possess another activation gate at the selectivity filter that can open widely enough to permeate large organic cations. Despite recent structural advances, the mechanism of selectivity filter gating and permeation for both metal ions and large molecules by TRPV1 or TRPV2 is not well known. Here, we determined two crystal structures of rabbit TRPV2 in its Ca(2+)-bound and resiniferatoxin (RTx)- and Ca(2+)-bound forms, to 3.9 A and 3.1 A, respectively. Notably, our structures show that RTx binding leads to two-fold symmetric opening of the selectivity filter of TRPV2 that is wide enough for large organic cation permeation. Combined with functional characterizations, our studies reveal a structural basis for permeation of Ca(2+) and large organic cations in TRPV2. Conformational plasticity in the selectivity filter of the TRPV2 ion channel.,Zubcevic L, Le S, Yang H, Lee SY Nat Struct Mol Biol. 2018 May;25(5):405-415. doi: 10.1038/s41594-018-0059-z. Epub, 2018 Apr 30. PMID:29728656 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ion channels 3D structures

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