5H9B

Drosophila CaMKII-wt in complex with a fragment of the Eag potassium channel and Mg2+/AMPPN

5H9B の概要

• エントリーDOI: 10.2210/pdb5h9b/pdb
• 分子名称: Calcium/calmodulin-dependent protein kinase II, isoform C, Potassium voltage-gated channel protein eag, AMP PHOSPHORAMIDATE, ... (6 entities in total)
• 機能のキーワード: protein kinase, potassium channel, complex, transferase
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38133.20

構造登録者

Castro-Rodrigues, A.F.,Morais-Cabral, J.H. (登録日: 2015-12-27, 公開日: 2017-01-11, 最終更新日: 2024-05-08)

主引用文献

Castro-Rodrigues, A.F.,Zhao, Y.,Fonseca, F.,Gabant, G.,Cadene, M.,Robertson, G.A.,Morais-Cabral, J.H.
The Interaction between the Drosophila EAG Potassium Channel and the Protein Kinase CaMKII Involves an Extensive Interface at the Active Site of the Kinase.
J.Mol.Biol., 430:5029-5049, 2018

PubMed Abstract: The Drosophila EAG (dEAG) potassium channel is the founding member of the superfamily of KNCH channels, which are involved in cardiac repolarization, neuronal excitability and cellular proliferation. In flies, dEAG is involved in regulation of neuron firing and assembles with CaMKII to form a complex implicated in memory formation. We have characterized the interaction between the kinase domain of CaMKII and a 53-residue fragment of the dEAG channel that includes a canonical CaMKII recognition sequence. Crystal structures together with biochemical/biophysical analysis show a substrate-kinase complex with an unusually tight and extensive interface that appears to be strengthened by phosphorylation of the channel fragment. Electrophysiological recordings show that catalytically active CaMKII is required to observe active dEAG channels. A previously identified phosphorylation site in the recognition sequence is not the substrate for this crucial kinase activity, but rather contributes importantly to the tight interaction of the kinase with the channel. The available data suggest that the dEAG channel is a docking platform for the kinase and that phosphorylation of the channel's kinase recognition sequence modulates the strength of the interaction between the channel and the kinase.

PubMed: 30381148
DOI: 10.1016/j.jmb.2018.10.015

実験手法

X-RAY DIFFRACTION (2.25 Å)