3KK8
CaMKII Substrate Complex A
Summary for 3KK8
Entry DOI | 10.2210/pdb3kk8/pdb |
Related | 3KK9 3KL8 |
Descriptor | Calcium/calmodulin dependent protein kinase II, MAGNESIUM ION (3 entities in total) |
Functional Keywords | protein kinase, atp-binding, kinase, nucleotide-binding, serine/threonine-protein kinase, transferase |
Biological source | Caenorhabditis elegans (nematode) |
Total number of polymer chains | 1 |
Total formula weight | 32227.89 |
Authors | Kuriyan, J.,Chao, L.H.,Pellicena, P.,Deindl, S.,Barclay, L.A.,Schulman, H. (deposition date: 2009-11-04, release date: 2010-02-09, Last modification date: 2021-10-13) |
Primary citation | Chao, L.H.,Pellicena, P.,Deindl, S.,Barclay, L.A.,Schulman, H.,Kuriyan, J. Intersubunit capture of regulatory segments is a component of cooperative CaMKII activation. Nat.Struct.Mol.Biol., 17:264-272, 2010 Cited by PubMed Abstract: The dodecameric holoenzyme of calcium-calmodulin-dependent protein kinase II (CaMKII) responds to high-frequency Ca(2+) pulses to become Ca(2+) independent. A simple coincidence-detector model for Ca(2+)-frequency dependency assumes noncooperative activation of kinase domains. We show that activation of CaMKII by Ca(2+)-calmodulin is cooperative, with a Hill coefficient of approximately 3.0, implying sequential kinase-domain activation beyond dimeric units. We present data for a model in which cooperative activation includes the intersubunit 'capture' of regulatory segments. Such a capture interaction is seen in a crystal structure that shows extensive contacts between the regulatory segment of one kinase and the catalytic domain of another. These interactions are mimicked by a natural inhibitor of CaMKII. Our results show that a simple coincidence-detection model cannot be operative and point to the importance of kinetic dissection of the frequency-response mechanism in future experiments. PubMed: 20139983DOI: 10.1038/nsmb.1751 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.72 Å) |
Structure validation
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