The CaMKII holoenzyme structure in activation-competent conformations
Ca2+/calmodulin-dependent protein kinase II (CaMKII) forms a 12 subunit holoenzyme central to synaptic plasticity. Here the authors report a 3D structure of the CaMKII holoenzyme in an activation-competent state obtained by single particle EM, and suggest a role for the intrinsically disordered link...
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2017-06-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/ncomms15742 |
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doaj-7852f7f279904d55b15ee9e82bae8fc72021-05-11T07:35:03ZengNature Publishing GroupNature Communications2041-17232017-06-018111510.1038/ncomms15742The CaMKII holoenzyme structure in activation-competent conformationsJanette B. Myers0Vincent Zaegel1Steven J. Coultrap2Adam P. Miller3K. Ulrich Bayer4Steve L. Reichow5Department of Chemistry, Portland State UniversityDepartment of Pharmacology, University of ColoradoDepartment of Pharmacology, University of ColoradoDepartment of Chemistry, Portland State UniversityDepartment of Pharmacology, University of ColoradoDepartment of Chemistry, Portland State UniversityCa2+/calmodulin-dependent protein kinase II (CaMKII) forms a 12 subunit holoenzyme central to synaptic plasticity. Here the authors report a 3D structure of the CaMKII holoenzyme in an activation-competent state obtained by single particle EM, and suggest a role for the intrinsically disordered linker domain in facilitating cooperative activation.https://doi.org/10.1038/ncomms15742 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Janette B. Myers Vincent Zaegel Steven J. Coultrap Adam P. Miller K. Ulrich Bayer Steve L. Reichow |
spellingShingle |
Janette B. Myers Vincent Zaegel Steven J. Coultrap Adam P. Miller K. Ulrich Bayer Steve L. Reichow The CaMKII holoenzyme structure in activation-competent conformations Nature Communications |
author_facet |
Janette B. Myers Vincent Zaegel Steven J. Coultrap Adam P. Miller K. Ulrich Bayer Steve L. Reichow |
author_sort |
Janette B. Myers |
title |
The CaMKII holoenzyme structure in activation-competent conformations |
title_short |
The CaMKII holoenzyme structure in activation-competent conformations |
title_full |
The CaMKII holoenzyme structure in activation-competent conformations |
title_fullStr |
The CaMKII holoenzyme structure in activation-competent conformations |
title_full_unstemmed |
The CaMKII holoenzyme structure in activation-competent conformations |
title_sort |
camkii holoenzyme structure in activation-competent conformations |
publisher |
Nature Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2017-06-01 |
description |
Ca2+/calmodulin-dependent protein kinase II (CaMKII) forms a 12 subunit holoenzyme central to synaptic plasticity. Here the authors report a 3D structure of the CaMKII holoenzyme in an activation-competent state obtained by single particle EM, and suggest a role for the intrinsically disordered linker domain in facilitating cooperative activation. |
url |
https://doi.org/10.1038/ncomms15742 |
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