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Backbone resonance assignments of the catalytic and regulatory domains of Ca(2+)/calmodulin-dependent protein kinase 1D
The CaMK subfamily of Ser/Thr kinases are regulated by calmodulin interactions with their C-terminal regions. They are exemplified by Ca(2+)/calmodulin dependent protein kinase 1δ which is known as CaMK1D, CaMKIδ or CKLiK. CaMK1D mediates intracellular signalling downstream of Ca(2+) influx and ther...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Netherlands
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7462902/ https://www.ncbi.nlm.nih.gov/pubmed/32535836 http://dx.doi.org/10.1007/s12104-020-09950-x |
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author | Tong, Michael H. G. Jeeves, Mark Rajesh, Sundaresan Ludwig, Christian Lenoir, Marc Kumar, Jitendra McClelland, Darren M. Berditchevski, Fedor Hubbard, Julia A. Kenyon, Colin Butterworth, Sam Knapp, Stefan Overduin, Michael |
author_facet | Tong, Michael H. G. Jeeves, Mark Rajesh, Sundaresan Ludwig, Christian Lenoir, Marc Kumar, Jitendra McClelland, Darren M. Berditchevski, Fedor Hubbard, Julia A. Kenyon, Colin Butterworth, Sam Knapp, Stefan Overduin, Michael |
author_sort | Tong, Michael H. G. |
collection | PubMed |
description | The CaMK subfamily of Ser/Thr kinases are regulated by calmodulin interactions with their C-terminal regions. They are exemplified by Ca(2+)/calmodulin dependent protein kinase 1δ which is known as CaMK1D, CaMKIδ or CKLiK. CaMK1D mediates intracellular signalling downstream of Ca(2+) influx and thereby exhibits amplifications of Ca(2+)signals and polymorphisms that have been implicated in breast cancer and diabetes. Here we report the backbone (1)H, (13)C, (15)N assignments of the 38 kDa human CaMK1D protein in its free state, including both the canonical bi-lobed kinase fold as well as the autoinhibitory and calmodulin binding domains. |
format | Online Article Text |
id | pubmed-7462902 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Springer Netherlands |
record_format | MEDLINE/PubMed |
spelling | pubmed-74629022020-09-11 Backbone resonance assignments of the catalytic and regulatory domains of Ca(2+)/calmodulin-dependent protein kinase 1D Tong, Michael H. G. Jeeves, Mark Rajesh, Sundaresan Ludwig, Christian Lenoir, Marc Kumar, Jitendra McClelland, Darren M. Berditchevski, Fedor Hubbard, Julia A. Kenyon, Colin Butterworth, Sam Knapp, Stefan Overduin, Michael Biomol NMR Assign Article The CaMK subfamily of Ser/Thr kinases are regulated by calmodulin interactions with their C-terminal regions. They are exemplified by Ca(2+)/calmodulin dependent protein kinase 1δ which is known as CaMK1D, CaMKIδ or CKLiK. CaMK1D mediates intracellular signalling downstream of Ca(2+) influx and thereby exhibits amplifications of Ca(2+)signals and polymorphisms that have been implicated in breast cancer and diabetes. Here we report the backbone (1)H, (13)C, (15)N assignments of the 38 kDa human CaMK1D protein in its free state, including both the canonical bi-lobed kinase fold as well as the autoinhibitory and calmodulin binding domains. Springer Netherlands 2020-06-13 2020 /pmc/articles/PMC7462902/ /pubmed/32535836 http://dx.doi.org/10.1007/s12104-020-09950-x Text en © The Author(s) 2020 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/. |
spellingShingle | Article Tong, Michael H. G. Jeeves, Mark Rajesh, Sundaresan Ludwig, Christian Lenoir, Marc Kumar, Jitendra McClelland, Darren M. Berditchevski, Fedor Hubbard, Julia A. Kenyon, Colin Butterworth, Sam Knapp, Stefan Overduin, Michael Backbone resonance assignments of the catalytic and regulatory domains of Ca(2+)/calmodulin-dependent protein kinase 1D |
title | Backbone resonance assignments of the catalytic and regulatory domains of Ca(2+)/calmodulin-dependent protein kinase 1D |
title_full | Backbone resonance assignments of the catalytic and regulatory domains of Ca(2+)/calmodulin-dependent protein kinase 1D |
title_fullStr | Backbone resonance assignments of the catalytic and regulatory domains of Ca(2+)/calmodulin-dependent protein kinase 1D |
title_full_unstemmed | Backbone resonance assignments of the catalytic and regulatory domains of Ca(2+)/calmodulin-dependent protein kinase 1D |
title_short | Backbone resonance assignments of the catalytic and regulatory domains of Ca(2+)/calmodulin-dependent protein kinase 1D |
title_sort | backbone resonance assignments of the catalytic and regulatory domains of ca(2+)/calmodulin-dependent protein kinase 1d |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7462902/ https://www.ncbi.nlm.nih.gov/pubmed/32535836 http://dx.doi.org/10.1007/s12104-020-09950-x |
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