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- W2023129668 abstract "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 Å 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." @default.
- W2023129668 created "2016-06-24" @default.
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- W2023129668 date "2005-12-01" @default.
- W2023129668 modified "2023-10-16" @default.
- W2023129668 title "Structure of the Autoinhibited Kinase Domain of CaMKII and SAXS Analysis of the Holoenzyme" @default.
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- W2023129668 doi "https://doi.org/10.1016/j.cell.2005.10.029" @default.
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