3KL8
CaMKIINtide Inhibitor Complex
3KL8 の概要
エントリーDOI | 10.2210/pdb3kl8/pdb |
関連するPDBエントリー | 3KK8 3KK9 |
分子名称 | Calcium/calmodulin dependent protein kinase II, Calcium/calmodulin-dependent protein kinase II inhibitor 1 (3 entities in total) |
機能のキーワード | camkii, camkiintide, atp-binding, kinase, nucleotide-binding, serine/threonine-protein kinase, cell junction, cell membrane, membrane, postsynaptic cell membrane, protein kinase inhibitor, synapse, synaptosome, transferase- transferase inhibitor complex, transferase/ transferase inhibitor |
由来する生物種 | Caenorhabditis elegans (nematode) 詳細 |
細胞内の位置 | Cell junction, synapse, synaptosome: Q9JI15 |
タンパク質・核酸の鎖数 | 10 |
化学式量合計 | 162321.00 |
構造登録者 | Kuriyan, J.,Chao, L.H.,Pellicena, P.,Deindl, S.,Barclay, L.A.,Schulman, H. (登録日: 2009-11-06, 公開日: 2010-02-09, 最終更新日: 2024-02-21) |
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 Cited by 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: 20139983DOI: 10.1038/nsmb.1751 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.372 Å) |
構造検証レポート
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