Structural highlights
Publication Abstract from PubMed
Transient receptor potential vanilloid (TRPV) cation channels are polymodal sensors involved in a variety of physiological processes. TRPV2, a member of the TRPV family, is regulated by temperature, by ligands, such as probenecid and cannabinoids, and by lipids. TRPV2 has been implicated in many biological functions, including somatosensation, osmosensation and innate immunity. Here we present the atomic model of rabbit TRPV2 in its putative desensitized state, as determined by cryo-EM at a nominal resolution of approximately 4 A. In the TRPV2 structure, the transmembrane segment 6 (S6), which is involved in gate opening, adopts a conformation different from the one observed in TRPV1. Structural comparisons of TRPV1 and TRPV2 indicate that a rotation of the ankyrin-repeat domain is coupled to pore opening via the TRP domain, and this pore opening can be modulated by rearrangements in the secondary structure of S6.
Cryo-electron microscopy structure of the TRPV2 ion channel.,Zubcevic L, Herzik MA Jr, Chung BC, Liu Z, Lander GC, Lee SY Nat Struct Mol Biol. 2016 Jan 18. doi: 10.1038/nsmb.3159. PMID:26779611[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zubcevic L, Herzik MA Jr, Chung BC, Liu Z, Lander GC, Lee SY. Cryo-electron microscopy structure of the TRPV2 ion channel. Nat Struct Mol Biol. 2016 Jan 18. doi: 10.1038/nsmb.3159. PMID:26779611 doi:http://dx.doi.org/10.1038/nsmb.3159
