2BDW

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

Summary for 2BDW

• Entry DOI: 10.2210/pdb2bdw/pdb
• Descriptor: Hypothetical protein K11E8.1d (2 entities in total)
• Functional Keywords: kinase; calmodulin activated, transferase
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 2
• Total formula weight: 81258.62

Authors

Rosenberg, O.S.,Kuriyan, J. (deposition date: 2005-10-20, release date: 2005-12-13, Last modification date: 2023-08-23)

Primary citation

Rosenberg, O.S.,Deindl, S.,Sung, R.-J.,Nairn, A.C.,Kuriyan, J.
Structure of the Autoinhibited Kinase Domain of CaMKII and SAXS Analysis of the Holoenzyme
Cell(Cambridge,Mass.), 123:849-860, 2005

PubMed 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 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.

PubMed: 16325579
DOI: 10.1016/j.cell.2005.10.029

Experimental method

X-RAY DIFFRACTION (1.8 Å)