2bdw

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spinqualitylabelsall models 2bdw, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of the Auto-Inhibited Kinase Domain of Calcium/Calmodulin Activated Kinase II

Overview

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.

About this Structure

2BDW is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.

Reference

Structure of the autoinhibited kinase domain of CaMKII and SAXS analysis of the holoenzyme., Rosenberg OS, Deindl S, Sung RJ, Nairn AC, Kuriyan J, Cell. 2005 Dec 2;123(5):849-60. PMID:16325579

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