5FG8
Drosophila CaMKII-wt in complex with a fragment of the Eag potassium channel and Mg2+/ADP
Summary for 5FG8
| Entry DOI | 10.2210/pdb5fg8/pdb |
| Descriptor | Calcium/calmodulin-dependent protein kinase type II alpha chain, Potassium voltage-gated channel protein eag, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total) |
| Functional Keywords | protein kinase, potassium channel, complex, transferase |
| Biological source | Drosophila melanogaster (Fruit fly) More |
| Total number of polymer chains | 2 |
| Total formula weight | 38226.28 |
| Authors | Castro-Rodrigues, A.F.,Morais-Cabral, J.H. (deposition date: 2015-12-20, release date: 2016-12-28, Last modification date: 2024-05-08) |
| Primary citation | 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 Cited by 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: 30381148DOI: 10.1016/j.jmb.2018.10.015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.955 Å) |
Structure validation
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