7lpc

Cryo-EM structure of full-length TRPV1 at 48 degrees Celsius

spinqualitylabelsall models 7lpc, resolution 3.06Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.06Å Ligands: 6OU, LBN, T7X, YFP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Transient receptor potential vanilloid member 1 (TRPV1) is a Ca(2+)-permeable cation channel that serves as the primary heat and capsaicin sensor in humans. Using cryo-EM, we have determined the structures of apo and capsaicin-bound full-length rat TRPV1 reconstituted into lipid nanodiscs over a range of temperatures. This has allowed us to visualize the noxious heat-induced opening of TRPV1 in the presence of capsaicin. Notably, noxious heat-dependent TRPV1 opening comprises stepwise conformational transitions. Global conformational changes across multiple subdomains of TRPV1 are followed by the rearrangement of the outer pore, leading to gate opening. Solvent-accessible surface area analyses and functional studies suggest that a subset of residues form an interaction network that is directly involved in heat sensing. Our study provides a glimpse of the molecular principles underlying noxious physical and chemical stimuli sensing by TRPV1, which can be extended to other thermal sensing ion channels. Heat-dependent opening of TRPV1 in the presence of capsaicin.,Kwon DH, Zhang F, Suo Y, Bouvette J, Borgnia MJ, Lee SY Nat Struct Mol Biol. 2021 Jul;28(7):554-563. doi: 10.1038/s41594-021-00616-3., Epub 2021 Jul 8. PMID:34239123 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ion channels 3D structures

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