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

Miki Tanaka, Kaori Hayakawa, Nozomi Ogawa, Tatsuki Kurokawa, Kenichi Kitanishi, Kenji Ite, Toshitaka Matsui, Yasuo Mori, Masaki Unno

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)130-137
Number of pages8
JournalActa Crystallographica Section F: Structural Biology Communications
Volume76
DOIs
Publication statusPublished - 2020 Mar 1

Keywords

  • TRPV1
  • akyrin-repeat domain
  • human
  • nonreducing conditions

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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