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Structure paper

TitleInclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate.
Journal, issue, pagesJ. Mol. Biol., Vol. 347, Page 399-414, Year 2005
Publish dateMay 7, 2002 (structure data deposition date)
AuthorsYde, C.W. / Ermakova, I. / Issinger, O.G. / Niefind, K.
External linksJ. Mol. Biol. / PubMed:15740749
MethodsX-ray diffraction
Resolution1.66 - 2 Å
Structure data

PDB-1lp4:
Crystal structure of a binary complex of the catalytic subunit of protein kinase CK2 with Mg-AMPPNP
Method: X-RAY DIFFRACTION / Resolution: 1.86 Å

PDB-1lpu:
Low Temperature Crystal Structure of the Apo-form of the catalytic subunit of protein kinase CK2 from Zea mays
Method: X-RAY DIFFRACTION / Resolution: 1.86 Å

PDB-1lr4:
Room Temperature Crystal Structure of the Apo-form of the catalytic subunit of protein kinase CK2 from Zea mays
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3juh:
Crystal structure of a mutant of human protein kinase CK2alpha with altered cosubstrate specificity
Method: X-RAY DIFFRACTION / Resolution: 1.66 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-HOH:
WATER

ChemComp-BEN:
BENZAMIDINE

ChemComp-CL:
Unknown entry

ChemComp-GOL:
GLYCEROL

Source
  • zea mays (maize)
  • homo sapiens (human)
KeywordsTRANSFERASE / protein kinase / CK2 / casein kinase 2 / dual-cosubstrate specificity / eukaryotic protein kinase / ATP-binding / Kinase / Nucleotide-binding / Phosphoprotein / Serine/threonine-protein kinase / Wnt signaling pathway

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