4FG8

Crystal structure of human calcium/calmodulin-dependent protein kinase I 1-315 in complex with ATP

Summary for 4FG8

• Entry DOI: 10.2210/pdb4fg8/pdb
• Related: 4FG7 4FG9 4FGB
• Descriptor: Calcium/calmodulin-dependent protein kinase type 1, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• Functional Keywords: camk, calmodulin, autoinhibition, regulation mechanism, kinase, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm (By similarity): Q14012
• Total number of polymer chains: 2
• Total formula weight: 72545.76

Authors

Zha, M.,Zhong, C.,Ou, Y.,Wang, J.,Han, L.,Ding, J. (deposition date: 2012-06-04, release date: 2013-01-23, Last modification date: 2023-09-13)

Primary citation

Zha, M.,Zhong, C.,Ou, Y.,Han, L.,Wang, J.,Ding, J.
Crystal structures of human CaMKIalpha reveal insights into the regulation mechanism of CaMKI.
Plos One, 7:e44828-e44828, 2012

PubMed Abstract: Human calcium/calmodulin-dependent protein kinase I (CaMKI) plays pivotal roles in the nervous system. The activity of human CaMKI is regulated by a regulatory region including an autoinhibitory segment and a CaM-binding segment. We report here four structures of three CaMKIα truncates in apo form and in complexes with ATP. In an apo, autoinhibited structure, the activation segment adopts a unique helical conformation which together with the autoinhibitory segment constrains helices αC and αD in inactive conformations, sequesters Thr177 from being phosphorylated, and occludes the substrate-binding site. In an ATP-bound, inactive structure, the activation segment is largely disordered and the CaM-binding segment protrudes out ready for CaM binding. In an ATP-bound, active structure, the regulatory region is dissociated from the catalytic core and the catalytic site assumes an active conformation. Detailed structural analyses reveal the interplay of the regulatory region, the activation segment, and the nucleotide-binding site in the regulation of CaMKI.

PubMed: 23028635
DOI: 10.1371/journal.pone.0044828

Experimental method

X-RAY DIFFRACTION (2.2 Å)