1HKX
Crystal structure of calcium/calmodulin-dependent protein kinase
Summary for 1HKX
Entry DOI | 10.2210/pdb1hkx/pdb |
Related | 1CDM |
Descriptor | CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II ALPHA CHAIN, 2,3-DIHYDROXY-1,4-DITHIOBUTANE, CHLORIDE ION, ... (5 entities in total) |
Functional Keywords | transferase, serine/threonine-protein kinase, calmodulin-binding, phosphorylation, atp-binding, alternative splicing |
Biological source | MUS MUSCULUS (MOUSE) |
Cellular location | Isoform Alpha KAP: Cytoplasm (Probable): P11798 |
Total number of polymer chains | 14 |
Total formula weight | 239043.04 |
Authors | Hoelz, A.,Nairn, A.C.,Kuriyan, J. (deposition date: 2003-03-12, release date: 2003-06-02, Last modification date: 2024-06-19) |
Primary citation | Hoelz, A.,Nairn, A.C.,Kuriyan, J. Crystal Structure of a Tetradecameric Assembly of the Association Domain of Ca2+/Calmodulin-Dependent Kinase II Mol.Cell, 11:1241-, 2003 Cited by PubMed Abstract: We report the crystal structure of the 143 residue association domain of Ca(2+)/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 light scattering. Individual protomers form wedge-shaped structures from which N-terminal helical segments that connect to the kinase domain extend 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. PubMed: 12769848DOI: 10.1016/S1097-2765(03)00171-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.65 Å) |
Structure validation
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