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Structure of the Autoinhibited Kinase Domain of CaMKII and SAXS Analysis of the Holoenzyme
Open accessAbstract
Ca2+/calmodulin-dependent protein kinase-II (CaMKII) is unique among protein kinases for its dodecameric assembly and its complex response to Ca2+. The crystal structure of the autoinhibited kinase domain of CaMKII, determined at 1.8 A resolution, reveals an unexpected dimeric organization in which the calmodulin-responsive regulatory segments form a coiled-coil strut that blocks peptide and ATP binding to the otherwise intrinsically active kinase domains. A threonine residue in the regulatory segment, which when phosphorylated renders CaMKII calmodulin independent, is held apart from the catalytic sites by the organization of the dimer. This ensures a strict Ca2+ dependence for initial activation. The structure of the kinase dimer, when combined with small-angle X-ray scattering data for the holoenzyme, suggests that inactive CaMKII forms tightly packed autoinhibited assemblies that convert upon activation into clusters of loosely tethered and independent kinase domains.
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“As is the case with many kinases, CaMKII contains an autoinhibitory regulatory segment (FIGURE 2, A, B1, AND B2) that binds across the substrate binding groove, whose structure and function have been delineated by peptides, mutations, and crystallography (71–77).”
From Synaptic memory and CaMKII (2023) · cites this paper as [76]
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A Dynamic Pathway for Calcium-Independent Activation of CaMKII by Methionine Oxidation
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Metadata
- Authors
- Rosenberg, O. S., Deindl, S., Sung, R.-J., Nairn, A. C., & Kuriyan, J.
- Affiliations
- Howard Hughes Medical Institute (US)
- Yale University (US)
- Corresponding author
- Kuriyan, John
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2005-12
- Volume
- 123
- Issue
- 5
- Pages
- 849-860
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2023129668
- Cited by
- 333
- References
- 53
- Citations by year
- 2026: 7 · 2025: 10 · 2024: 14 · 2023: 21 · 2022: 16 · 2021: 14 · 2020: 20 · 2019: 14 · 2018: 11 · 2017: 9 · 2016: 7 · 2015: 13 · 2014: 13 · 2013: 13 · 2012: 22
- FWCI
- 8.44
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Keywords
- CaMKII, calcium/calmodulin-dependent protein kinase II, autoinhibition, kinase domain, threonine phosphorylation, calcium dependence, holoenzyme structure, protein kinase activation
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Calcium, Calmodulin, Models, Molecular, Molecular Sequence Data, Sequence Alignment, Caenorhabditis elegans, Protein Structure, Secondary, Protein Structure, Tertiary, Calcium-Calmodulin-Dependent Protein Kinases, Crystallography, X-Ray, Dimerization, Holoenzymes, Protein Structure, Quaternary, Caenorhabditis elegans Proteins, Calcium-Calmodulin-Dependent Protein Kinase Type 2
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