The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
A Mechanism for Tunable Autoinhibition in the Structure of a Human Ca2+/Calmodulin- Dependent Kinase II Holoenzyme
Open accessAbstract
Summary Calcium/calmodulin-dependent kinase II (CaMKII) forms a highly conserved dodecameric assembly that is sensitive to the frequency of calcium pulse trains. Neither the structure of the dodecameric assembly nor how it regulates CaMKII are known. We present the crystal structure of an autoinhibited full-length human CaMKII holoenzyme, revealing an unexpected compact arrangement of kinase domains docked against a central hub, with the calmodulin binding sites completely inaccessible. We show that this compact docking is important for the autoinhibition of the kinase domains and for setting the calcium response of the holoenzyme. Comparison of CaMKII isoforms, which differ in the length of the linker between the kinase domain and the hub, demonstrates that these interactions can be strengthened or weakened by changes in linker length. This equilibrium between autoinhibited states provides a simple mechanism for tuning the calcium response without changes in either the hub or the kinase domains.
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Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,715
Jones, T. A., Zou, J. Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,648
Gillespie, D. T. (1976) · Journal of Computational Physics · doi:10.1016/0021-9991(76)90041-3 · Cited by 6,029
PHENIX : building new software for automated crystallographic structure determination
Adams, P. D., Grosse-Kunstleve, R. W., Hung, L.-W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., & Terwilliger, T. C. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902016657 · Cited by 4,361
Malenka, R. C., & Bear, M. F. (2004) · Neuron · doi:10.1016/j.neuron.2004.09.012 · Cited by 3,968
Svergun, D. I. (1992) · Journal of Applied Crystallography · doi:10.1107/s0021889892001663 · Cited by 3,759
Svergun, D., Barberato, C., & Koch, M. H. J. (1995) · Journal of Applied Crystallography · doi:10.1107/s0021889895007047 · Cited by 3,434
PRIMUS: a Windows PC-based system for small-angle scattering data analysis
Konarev, P. V., Volkov, V. V., Sokolova, A. V., Koch, M. H. J., & Svergun, D. I. (2003) · Journal of Applied Crystallography · doi:10.1107/s0021889803012779 · Cited by 2,879
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Reiner, A., & Levitz, J. (2018) · Neuron · doi:10.1016/j.neuron.2018.05.018 · Cited by 631
Self-citationCaMKII: a central molecular organizer of synaptic plasticity, learning and memory
Yasuda, R., Hayashi, Y., & Hell, J. W. (2022) · Nature Reviews Neuroscience · doi:10.1038/s41583-022-00624-2 · Cited by 431
CaMKII: Claiming Center Stage in Postsynaptic Function and Organization
Hell, J. W. (2014) · Neuron · doi:10.1016/j.neuron.2013.12.024 · Cited by 358
Mechanisms of Altered Ca 2+ Handling in Heart Failure
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Metadata
- Authors
- Chao, L. H., Stratton, M. M., Lee, I.-H., Rosenberg, O. S., Levitz, J., Mandell, D. J., Kortemme, T., Groves, J. T., Schulman, H., & Kuriyan, J.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2011-09
- Volume
- 146
- Issue
- 5
- Pages
- 732-745
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2163978292
- Cited by
- 255
- References
- 59
- FWCI
- 7.41
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Chao, L. H., Stratton, M. M., Lee, I.-H., Rosenberg, O. S., Levitz, J., Mandell, D. J., Kortemme, T., Groves, J. T., Schulman, H., & Kuriyan, J. (2011). A Mechanism for Tunable Autoinhibition in the Structure of a Human Ca2+/Calmodulin- Dependent Kinase II Holoenzyme. Cell. https://doi.org/10.1016/j.cell.2011.07.038
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