TY - JOUR
T1 - Structure determination of the human TRPV1 ankyrin-repeat domain under nonreducing conditions
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
N1 - Publisher Copyright:
© 2020.
PY - 2020/3/1
Y1 - 2020/3/1
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.
KW - TRPV1
KW - akyrin-repeat domain
KW - human
KW - nonreducing conditions
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U2 - 10.1107/S2053230X20001533
DO - 10.1107/S2053230X20001533
M3 - Article
C2 - 32133998
AN - SCOPUS:85081041345
VL - 76
SP - 130
EP - 137
JO - Acta Crystallographica Section F:Structural Biology Communications
JF - Acta Crystallographica Section F:Structural Biology Communications
SN - 1744-3091
ER -