3KK9

CaMKII Substrate Complex B

3KK9 の概要

• エントリーDOI: 10.2210/pdb3kk9/pdb
• 関連するPDBエントリー: 3KK8 3KL8
• 分子名称: Calcium/calmodulin dependent protein kinase II (1 entity in total)
• 機能のキーワード: camkii, atp-binding, kinase, nucleotide-binding, serine/threonine-protein kinase, transferase
• 由来する生物種: Caenorhabditis elegans (nematode)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32003.35

構造登録者

Kuriyan, J.,Chao, L.H.,Pellicena, P.,Deindl, S.,Barclay, L.A.,Schulman, H. (登録日: 2009-11-04, 公開日: 2010-02-09, 最終更新日: 2024-11-27)

主引用文献

Chao, L.H.,Pellicena, P.,Deindl, S.,Barclay, L.A.,Schulman, H.,Kuriyan, J.
Intersubunit capture of regulatory segments is a component of cooperative CaMKII activation.
Nat.Struct.Mol.Biol., 17:264-272, 2010

PubMed Abstract: The dodecameric holoenzyme of calcium-calmodulin-dependent protein kinase II (CaMKII) responds to high-frequency Ca(2+) pulses to become Ca(2+) independent. A simple coincidence-detector model for Ca(2+)-frequency dependency assumes noncooperative activation of kinase domains. We show that activation of CaMKII by Ca(2+)-calmodulin is cooperative, with a Hill coefficient of approximately 3.0, implying sequential kinase-domain activation beyond dimeric units. We present data for a model in which cooperative activation includes the intersubunit 'capture' of regulatory segments. Such a capture interaction is seen in a crystal structure that shows extensive contacts between the regulatory segment of one kinase and the catalytic domain of another. These interactions are mimicked by a natural inhibitor of CaMKII. Our results show that a simple coincidence-detection model cannot be operative and point to the importance of kinetic dissection of the frequency-response mechanism in future experiments.

PubMed: 20139983
DOI: 10.1038/nsmb.1751

実験手法

X-RAY DIFFRACTION (3.206 Å)