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

ABSTRACT: The aim of the project was to characterize structural changes that occur on the rod cyclic nucleotide-gated channel upon interaction with calmodulin (CaM) directly in the native membrane.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Bos Taurus (bovine)

SUBMITTER: Dina Schuster

LAB HEAD: Volodymyr M. Korkhov

PROVIDER: PXD038768 | Pride | 2023-04-06

REPOSITORIES: Pride

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			Action	DRS
	20221007_142048_dschuster_CNG_TC.sne	Other
	20221007_142430_dschuster_CNG_TC_Report.csv	Csv
	20221007_142430_dschuster_CNG_TC_Report.log.txt	Txt
	20221007_142430_dschuster_CNG_TC_Report.params	Other
	20221007_142430_dschuster_CNG_TC_Report.setup.txt	Txt

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Publications

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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