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Structural insight into TRPV5 channel function and modulation

delete2019-04-11
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OA
AI
S
Shangyu Dang
M
Mark K. van Goor
D
Daniel Asarnow
Y
Yongqiang Wang
D
David Julius *
Y
Yifan Cheng *
J
Jenny van der Wijst *
DOI:10.1073/pnas.1820323116delete
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Abstract

Abstract

En 中文
TRPV5 (transient receptor potential vanilloid 5) is a unique calcium-selective TRP channel essential for calcium homeostasis. Unlike other TRPV channels, TRPV5 and its close homolog, TRPV6, do not exhibit thermosensitivity or ligand-dependent activation but are constitutively open at physiological membrane potentials and modulated by calmodulin (CaM) in a calcium-dependent manner. Here we report high-resolution electron cryomicroscopy structures of truncated and full-length TRPV5 in lipid nanodiscs, as well as of a TRPV5 W583A mutant and TRPV5 in complex with CaM. These structures highlight the mechanism of calcium regulation and reveal a flexible stoichiometry of CaM binding to TRPV5.
Keywords:
TRP channel
calcium
calmodulin
cryo-EM
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Journal

P
Proceedings of the National Academy of Sciences of the United States of America
IF:
9.1
Papers:
10.8W
Citations:
73.5W

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H
Howard Hughes Medical Institute
Scholars:
1.2W
Papers: 7.8K
Citations: 6.0W
University of California System cover
University of California System
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37.5W
Papers: 33.7W
Citations: 6.6K
R
Radboud University Nijmegen
Scholars:
4.4W
Papers: 3.4W
Citations: 5.4W
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