3soa | pdb_00003soa

Full-length human CaMKII

spinqualitylabelsall models 3soa, resolution 3.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3soa is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: DB8 Gene: camk2a, camka, kiaa0968, camk2b, camkb (HUMAN) Activity: Calcium/calmodulin-dependent protein kinase, with EC number 2.7.11.17 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [KCC2A_HUMAN] CaM-kinase II (CAMK2) is a prominent kinase in the central nervous system that may function in long-term potentiation and neurotransmitter release. Member of the NMDAR signaling complex in excitatory synapses it may regulate NMDAR-dependent potentiation of the AMPAR and synaptic plasticity (By similarity). Publication Abstract from PubMed 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. PAPERFLICK: A Mechanism for Tunable Autoinhibition in the Structure of a Human Ca(2+)/Calmodulin- Dependent Kinase II Holoenzyme.,Chao LH, Stratton MM, Lee IH, Rosenberg OS, Levitz J, Mandell DJ, Kortemme T, Groves JT, Schulman H, Kuriyan J Cell. 2011 Sep 2;146(5):732-45. PMID:21884935 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Calcium/calmodulin dependent protein kinase 3D structures

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