4FG8

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

4FG8 の概要

• エントリーDOI: 10.2210/pdb4fg8/pdb
• 関連するPDBエントリー: 4FG7 4FG9 4FGB
• 分子名称: Calcium/calmodulin-dependent protein kinase type 1, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: camk, calmodulin, autoinhibition, regulation mechanism, kinase, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm (By similarity): Q14012
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 72545.76

構造登録者

Zha, M.,Zhong, C.,Ou, Y.,Wang, J.,Han, L.,Ding, J. (登録日: 2012-06-04, 公開日: 2013-01-23, 最終更新日: 2023-09-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)