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Structure paper

TitlePKA-I holoenzyme structure reveals a mechanism for cAMP-dependent activation.
Journal, issue, pagesCell(Cambridge,Mass. ), Vol. 130, Page 1032-1043, Year 2007
Publish dateJun 19, 2007 (structure data deposition date)
AuthorsKim, C. / Cheng, C.Y. / Saldanha, S.A. / Taylor, S.S.
External linksCell(Cambridge,Mass. ) / PubMed:17889648
MethodsX-ray diffraction
Resolution2.2 Å
Structure data

PDB-2qcs:
A complex structure between the Catalytic and Regulatory subunit of Protein Kinase A that represents the inhibited state
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-ACT:
ACETATE ION

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

ChemComp-TAM:
TRIS(HYDROXYETHYL)AMINOMETHANE / pH buffer*YM

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • mus musculus (house mouse)
  • bos taurus (domestic cattle)
KeywordsTRANSFERASE/TRANSFERASE INHIBITOR / cyclic adenosine monophosphate / cAMP-dependent protein kinase / PKA holoenzyme / cyclic nucleotide binding domain / protein-protein interaction / conformational change / PROTEIN BINDING / TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX

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