5fg8

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

Structural highlights 5fg8 is a 2 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.955Å Ligands: , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KCC2A_DROME A key regulator of plasticity in synaptic physiology and behavior, alterations in its activity produce pleiotrophic effects that involve synaptic transmission and development as well as various aspects of behavior. Directly modulates eag potassium channels. Publication Abstract from PubMed 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. The Interaction between the Drosophila EAG Potassium Channel and the Protein Kinase CaMKII Involves an Extensive Interface at the Active Site of the Kinase.,Castro-Rodrigues AF, Zhao Y, Fonseca F, Gabant G, Cadene M, Robertson GA, Morais-Cabral JH J Mol Biol. 2018 Dec 7;430(24):5029-5049. doi: 10.1016/j.jmb.2018.10.015. Epub, 2018 Oct 28. PMID:30381148 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Calcium/calmodulin dependent protein kinase 3D structures Potassium channel 3D structures

spinqualitylabelsall models 5fg8, resolution 1.96Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image