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

doi:10.1107/S2053230X20001533

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

Division of Organic- and Biomaterials Research

Research output: Contribution to journal › Article › peer-review

1 Citation (Scopus)

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 language	English
Pages (from-to)	130-137
Number of pages	8
Journal	Acta Crystallographica Section F: Structural Biology Communications
Volume	76
DOIs	https://doi.org/10.1107/S2053230X20001533
Publication status	Published - 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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Structure determination of the human TRPV1 ankyrin-repeat domain under nonreducing conditions. / Tanaka, Miki; Hayakawa, Kaori; Ogawa, Nozomi; Kurokawa, Tatsuki; Kitanishi, Kenichi; Ite, Kenji; Matsui, Toshitaka; Mori, Yasuo; Unno, Masaki.

In: Acta Crystallographica Section F: Structural Biology Communications, Vol. 76, 01.03.2020, p. 130-137.

Research output: Contribution to journal › Article › peer-review

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title = "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 {\AA} 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.",

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AU - Tanaka, Miki

AU - Hayakawa, Kaori

AU - Ogawa, Nozomi

AU - Kurokawa, Tatsuki

AU - Kitanishi, Kenichi

AU - Ite, Kenji

AU - Matsui, Toshitaka

AU - Mori, Yasuo

AU - Unno, Masaki

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N2 - 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.

AB - 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.

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KW - nonreducing conditions

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

Abstract

Keywords

ASJC Scopus subject areas

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