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Structural basis of calmodulin modulation of the rod cyclic nucleotide-gated channel (XL-MS)

ABSTRACT: We used chemical crosslinking mass spectrometry to study the organization and the interaction of the bovine rod outer segment cyclic nugleotide-gated channel with calmodulin. The aims of the study were to identify the D-helix that could not be resolved with cryo-EM and gain further insights into the protein organization.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Bos Taurus (bovine)

SUBMITTER: Dina Schuster

LAB HEAD: Volodymyr M. Korkhov

PROVIDER: PXD038640 | Pride | 2023-04-06

REPOSITORIES: Pride

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Structural basis of calmodulin modulation of the rod cyclic nucleotide-gated channel.

Barret Diane C A DCA Schuster Dina D Rodrigues Matthew J MJ Leitner Alexander A Picotti Paola P Schertler Gebhard F X GFX Kaupp U Benjamin UB Korkhov Volodymyr M VM Marino Jacopo J

Proceedings of the National Academy of Sciences of the United States of America 20230403 15

Calmodulin (CaM) regulates many ion channels to control calcium entry into cells, and mutations that alter this interaction are linked to fatal diseases. The structural basis of CaM regulation remains largely unexplored. In retinal photoreceptors, CaM binds to the CNGB subunit of cyclic nucleotide-gated (CNG) channels and, thereby, adjusts the channel's Cyclic guanosine monophosphate (cGMP) sensitivity in response to changes in ambient light conditions. Here, we provide the structural characteri ...[more]

PMID: 37011209

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