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Structure paper

TitleCyclic AMP analog blocks kinase activation by stabilizing inactive conformation: conformational selection highlights a new concept in allosteric inhibitor design.
Journal, issue, pagesMol. Cell Proteomics, Vol. 10, Page M110.004390-M110.004390, Year 2011
Publish dateJul 31, 2009 (structure data deposition date)
AuthorsBadireddy, S. / Yunfeng, G. / Ritchie, M. / Akamine, P. / Wu, J. / Kim, C.W. / Taylor, S.S. / Qingsong, L. / Swaminathan, K. / Anand, G.S.
External linksMol. Cell Proteomics / PubMed:21081668
MethodsX-ray diffraction
Resolution1.503 - 2.7 Å
Structure data

PDB-3iia:
Crystal structure of apo (91-244) RIa subunit of cAMP-dependent protein kinase
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-3pna:
Crystal Structure of cAMP bound (91-244)RIa Subunit of cAMP-dependent Protein Kinase
Method: X-RAY DIFFRACTION / Resolution: 1.503 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-CMP:
ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE

Source
  • bos taurus (domestic cattle)
KeywordsTRANSFERASE / protein kinase A / cyclic AMP / RIa subunit / cAMP / cAMP-binding / Disulfide bond / Nucleotide-binding / Phosphoprotein / beta-barrel / catalytic subunit

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