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Structure determination of the human TRPV1 ankyrin‐repeat domain under nonreducing conditions
Author(s) -
Tanaka Miki,
Hayakawa Kaori,
Ogawa Nozomi,
Kurokawa Tatsuki,
Kitanishi Kenichi,
Ite Kenji,
Matsui Toshitaka,
Mori Yasuo,
Unno Masaki
Publication year - 2020
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x20001533
Subject(s) - trpv1 , ankyrin repeat , transient receptor potential channel , ankyrin , chemistry , biophysics , ligand (biochemistry) , conformational change , protein subunit , biochemistry , crystallography , stereochemistry , receptor , biology , gene
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.