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Structure determination of the human TRPV1 ankyrin-repeat domain under nonreducing conditions.

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.

SUBMITTER: Tanaka M

PROVIDER: S-EPMC7057350 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

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Structure determination of the human TRPV1 ankyrin-repeat domain under nonreducing conditions.

Tanaka Miki M Hayakawa Kaori K Ogawa Nozomi N Kurokawa Tatsuki T Kitanishi Kenichi K Ite Kenji K Matsui Toshitaka T Mori Yasuo Y Unno Masaki M

Acta crystallographica. Section F, Structural biology communications 20200302 Pt 3

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 i ...[more]

PMID: 32133998

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