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Crystal Structure of a Tetradecameric Assembly of the Association Domain of Ca2+/Calmodulin-Dependent Kinase II

Andre Hoelz, Angus C. Nairn, and John Kuriyan

Molecular Cell (2003) May: 1241-1251

Abstract / Figures / PDB coordinates


We report the crystal structure of the 143 residue association domain of Ca2+/calmodulin-dependent protein kinase II (CaMKII). The association domain forms a hub-like assembly, composed of two rings of seven protomers each, which are stacked head to head and held together by extensive interfaces. The tetradecameric organization of the assembly was confirmed by analytical ultracentrifugation and multiangle scattering. Individual protomers form wedge-shaped structures from which N-terminal helical segments that connect to the kinase domain extent toward the equatorial plane of the assembly, consistent with the arrangement of the kinase domains in a second outer ring. A deep and highly conserved pocket present within the association domain may serve as a docking site for proteins that interact with CaMKII.

Figures (Click on the small image to get a bigger one):

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Supplemental Figure 1

Supplemental Figure 2

Crystals and Diffraction

Map 1

Map 2

Patterson Self Rotation Function

Ramachandran Plot

PDB Coordinates:

1HKX, Crystal Structure of Calcium/Calmodulin -Dependent Protein Kinase