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Cryo-EM structure of TRPV5 with calmodulin bound

ABSTRACT:

SUBMITTER: Shangyu Dang

PROVIDER: EMPIAR-10256 | biostudies-other |

REPOSITORIES: biostudies-other

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Structural insight into TRPV5 channel function and modulation.

Dang Shangyu S van Goor Mark K MK Asarnow Daniel D Wang YongQiang Y Julius David D Cheng Yifan Y van der Wijst Jenny J

Proceedings of the National Academy of Sciences of the United States of America 20190411 18

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 nanodi ...[more]

PMID: 30975749

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