6dvz

Cryo-EM structure of mouse TRPV3-Y564A in complex with 2-Aminoethoxydiphenyl borate (2-APB)Cryo-EM structure of mouse TRPV3-Y564A in complex with 2-Aminoethoxydiphenyl borate (2-APB)

6dvz, resolution 4.24Å Show:Asymmetric Unit Biological Assembly Structural highlights 6dvz is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 4.24Å Ligands: Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TRPV3_MOUSE Putative receptor-activated non-selective calcium permeant cation channel. It is activated by innocuous (warm) temperatures and shows an increased response at noxious temperatures greater than 39 degrees Celsius. Activation exhibits an outward rectification. May associate with TRPV1 and may modulate its activity. Is a negative regulator of hair growth and cycling: TRPV3-coupled signaling suppresses keratinocyte proliferation in hair follicles and induces apoptosis and premature hair follicle regression (catagen) (By similarity). Publication Abstract from PubMed Transient receptor potential vanilloid subfamily member 3 (TRPV3) channel plays a crucial role in skin physiology and pathophysiology. Mutations in TRPV3 are associated with various skin diseases, including Olmsted syndrome, atopic dermatitis, and rosacea. Here we present the cryo-electron microscopy structures of full-length mouse TRPV3 in the closed apo and agonist-bound open states. The agonist binds three allosteric sites distal to the pore. Channel opening is accompanied by conformational changes in both the outer pore and the intracellular gate. The gate is formed by the pore-lining S6 helices that undergo local alpha-to-pi helical transitions, elongate, rotate, and splay apart in the open state. In the closed state, the shorter S6 segments are entirely alpha-helical, expose their nonpolar surfaces to the pore, and hydrophobically seal the ion permeation pathway. These findings further illuminate TRP channel activation and can aid in the design of drugs for the treatment of inflammatory skin conditions, itch, and pain. Structure and gating mechanism of the transient receptor potential channel TRPV3.,Singh AK, McGoldrick LL, Sobolevsky AI Nat Struct Mol Biol. 2018 Sep;25(9):805-813. doi: 10.1038/s41594-018-0108-7. Epub, 2018 Aug 20. PMID:30127359 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ion channels 3D structures