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Structure paper

TitleThe Interaction between the Drosophila EAG Potassium Channel and the Protein Kinase CaMKII Involves an Extensive Interface at the Active Site of the Kinase.
Journal, issue, pagesJ. Mol. Biol., Vol. 430, Page 5029-5049, Year 2018
Publish dateDec 20, 2015 (structure data deposition date)
AuthorsCastro-Rodrigues, A.F. / Zhao, Y. / Fonseca, F. / Gabant, G. / Cadene, M. / Robertson, G.A. / Morais-Cabral, J.H.
External linksJ. Mol. Biol. / PubMed:30381148
MethodsX-ray diffraction
Resolution1.885 - 2.25 Å
Structure data

PDB-5fg8:
Drosophila CaMKII-wt in complex with a fragment of the Eag potassium channel and Mg2+/ADP
Method: X-RAY DIFFRACTION / Resolution: 1.955 Å

PDB-5h9b:
Drosophila CaMKII-wt in complex with a fragment of the Eag potassium channel and Mg2+/AMPPN
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-5hu3:
Drosophila CaMKII-D136N in complex with a phosphorylated fragment of the Eag potassium channel and Mg2+/ADP
Method: X-RAY DIFFRACTION / Resolution: 1.885 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-AN2:
AMP PHOSPHORAMIDATE

Source
  • drosophila melanogaster (fruit fly)
KeywordsTRANSFERASE / protein kinase / potassium channel / complex

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