Chemical shift assignments of calmodulin bound to the GluN1 C0 domain (residues 841–865) of the NMDA receptor

Neuroplasticity and synaptic transmission in the brain are regulated by N-methyl-D-aspartate receptors (NMDARs) that consist of hetero-tetrameric combinations of the glycine-binding GluN1 and glutamate-binding GluN2 subunits. Calmodulin (CaM) binds to the cytosolic C0 domain of GluN1 (residues 841–8...

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Autores principales: Bej, Aritra, Ames, James B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2023
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10232624/
https://www.ncbi.nlm.nih.gov/pubmed/36739573
http://dx.doi.org/10.1007/s12104-023-10121-x
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author Bej, Aritra
Ames, James B.
author_facet Bej, Aritra
Ames, James B.
author_sort Bej, Aritra
collection PubMed
description Neuroplasticity and synaptic transmission in the brain are regulated by N-methyl-D-aspartate receptors (NMDARs) that consist of hetero-tetrameric combinations of the glycine-binding GluN1 and glutamate-binding GluN2 subunits. Calmodulin (CaM) binds to the cytosolic C0 domain of GluN1 (residues 841–865) that may play a role in the Ca(2+)-dependent inactivation (CDI) of NMDAR channel activity. Dysregulation of NMDARs are linked to various neurological disorders, including Alzheimer’s disease, depression, stroke, epilepsy, and schizophrenia. Here, we report complete NMR chemical shift assignments of Ca(2+)-saturated CaM bound to the GluN1 C0 domain of the human NMDAR (BMRB no. 51715).
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spelling pubmed-102326242023-06-02 Chemical shift assignments of calmodulin bound to the GluN1 C0 domain (residues 841–865) of the NMDA receptor Bej, Aritra Ames, James B. Biomol NMR Assign Article Neuroplasticity and synaptic transmission in the brain are regulated by N-methyl-D-aspartate receptors (NMDARs) that consist of hetero-tetrameric combinations of the glycine-binding GluN1 and glutamate-binding GluN2 subunits. Calmodulin (CaM) binds to the cytosolic C0 domain of GluN1 (residues 841–865) that may play a role in the Ca(2+)-dependent inactivation (CDI) of NMDAR channel activity. Dysregulation of NMDARs are linked to various neurological disorders, including Alzheimer’s disease, depression, stroke, epilepsy, and schizophrenia. Here, we report complete NMR chemical shift assignments of Ca(2+)-saturated CaM bound to the GluN1 C0 domain of the human NMDAR (BMRB no. 51715). Springer Netherlands 2023-02-05 2023 /pmc/articles/PMC10232624/ /pubmed/36739573 http://dx.doi.org/10.1007/s12104-023-10121-x Text en © The Author(s) 2023 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 GluN1 C0 domain (residues 841–865) of the NMDA receptor
title Chemical shift assignments of calmodulin bound to the GluN1 C0 domain (residues 841–865) of the NMDA receptor
title_full Chemical shift assignments of calmodulin bound to the GluN1 C0 domain (residues 841–865) of the NMDA receptor
title_fullStr Chemical shift assignments of calmodulin bound to the GluN1 C0 domain (residues 841–865) of the NMDA receptor
title_full_unstemmed Chemical shift assignments of calmodulin bound to the GluN1 C0 domain (residues 841–865) of the NMDA receptor
title_short Chemical shift assignments of calmodulin bound to the GluN1 C0 domain (residues 841–865) of the NMDA receptor
title_sort chemical shift assignments of calmodulin bound to the glun1 c0 domain (residues 841–865) of the nmda receptor
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10232624/
https://www.ncbi.nlm.nih.gov/pubmed/36739573
http://dx.doi.org/10.1007/s12104-023-10121-x
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