Chemical shift assignments of calmodulin bound to the β-subunit of a retinal cyclic nucleotide-gated channel (CNGB1)

Rod cyclic nucleotide-gated (CNG) channels are formed by two protein subunits (CNGA1 and CNGB1). Calmodulin (CaM) binds to the cytosolic regulatory domain of CNGB1 and decreases the open probability of CNGA1/CNGB1 channels. The CaM binding site within bovine CNGB1 (residues 679–702) binds tightly to...

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Autores principales: Bej, Aritra, Ames, James B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2022
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9068646/
https://www.ncbi.nlm.nih.gov/pubmed/35107779
http://dx.doi.org/10.1007/s12104-022-10072-9
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author Bej, Aritra
Ames, James B.
author_facet Bej, Aritra
Ames, James B.
author_sort Bej, Aritra
collection PubMed
description Rod cyclic nucleotide-gated (CNG) channels are formed by two protein subunits (CNGA1 and CNGB1). Calmodulin (CaM) binds to the cytosolic regulatory domain of CNGB1 and decreases the open probability of CNGA1/CNGB1 channels. The CaM binding site within bovine CNGB1 (residues 679–702) binds tightly to Ca(2+)-bound CaM, which promotes Ca(2+)-induced inactivation of CNGA1/CNGB1 channels in retinal rods. We report complete NMR chemical shift assignments of Ca(2+)-saturated CaM bound to the CaM-binding domain of CNGB1 (BMRB no. 51222).
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spelling pubmed-90686462022-05-07 Chemical shift assignments of calmodulin bound to the β-subunit of a retinal cyclic nucleotide-gated channel (CNGB1) Bej, Aritra Ames, James B. Biomol NMR Assign Article Rod cyclic nucleotide-gated (CNG) channels are formed by two protein subunits (CNGA1 and CNGB1). Calmodulin (CaM) binds to the cytosolic regulatory domain of CNGB1 and decreases the open probability of CNGA1/CNGB1 channels. The CaM binding site within bovine CNGB1 (residues 679–702) binds tightly to Ca(2+)-bound CaM, which promotes Ca(2+)-induced inactivation of CNGA1/CNGB1 channels in retinal rods. We report complete NMR chemical shift assignments of Ca(2+)-saturated CaM bound to the CaM-binding domain of CNGB1 (BMRB no. 51222). Springer Netherlands 2022-02-02 2022 /pmc/articles/PMC9068646/ /pubmed/35107779 http://dx.doi.org/10.1007/s12104-022-10072-9 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Bej, Aritra
Ames, James B.
Chemical shift assignments of calmodulin bound to the β-subunit of a retinal cyclic nucleotide-gated channel (CNGB1)
title Chemical shift assignments of calmodulin bound to the β-subunit of a retinal cyclic nucleotide-gated channel (CNGB1)
title_full Chemical shift assignments of calmodulin bound to the β-subunit of a retinal cyclic nucleotide-gated channel (CNGB1)
title_fullStr Chemical shift assignments of calmodulin bound to the β-subunit of a retinal cyclic nucleotide-gated channel (CNGB1)
title_full_unstemmed Chemical shift assignments of calmodulin bound to the β-subunit of a retinal cyclic nucleotide-gated channel (CNGB1)
title_short Chemical shift assignments of calmodulin bound to the β-subunit of a retinal cyclic nucleotide-gated channel (CNGB1)
title_sort chemical shift assignments of calmodulin bound to the β-subunit of a retinal cyclic nucleotide-gated channel (cngb1)
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9068646/
https://www.ncbi.nlm.nih.gov/pubmed/35107779
http://dx.doi.org/10.1007/s12104-022-10072-9
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