| Literature DB >> 32133998 |
Miki Tanaka1, Kaori Hayakawa1, Nozomi Ogawa2, Tatsuki Kurokawa2, Kenichi Kitanishi1, Kenji Ite1, Toshitaka Matsui3, Yasuo Mori2, Masaki Unno1.
Abstract
TRPV1, a member of the transient receptor potential (TRP) channels family, has been found to be involved in redox sensing. The crystal structure of the human TRPV1 ankyrin-repeat domain (TRPV1-ARD) was determined at 4.5 Å resolution under nonreducing conditions. This is the first report of the crystal structure of a ligand-free form of TRPV1-ARD and in particular of the human homologue. The structure showed a unique conformation in finger loop 3 near Cys258, which is most likely to be involved in inter-subunit disulfide-bond formation. Also, in human TRPV1-ARD it was possible for solvent to access Cys258. This structural feature might be related to the high sensitivity of human TRPV1 to oxidants. ESI-MS revealed that Cys258 did not form an S-OH functionality even under nonreducing conditions.Entities:
Keywords: TRPV1; akyrin-repeat domain; human; nonreducing conditions
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Year: 2020 PMID： 32133998 PMCID： PMC7057350 DOI： 10.1107/S2053230X20001533
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN： 2053-230X Impact factor: 1.056