Structural highlights
Function
IPKA_HUMAN Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
6-phenylpurines were identified as novel, ATP-competitive inhibitors of protein kinase B (PKB/Akt) from a fragment-based screen and were rapidly progressed to potent compounds using iterative protein-ligand crystallography with a PKA-PKB chimeric protein. An elaborated lead compound showed cell growth inhibition and effects on cellular signaling pathways characteristic of PKB inhibition.
Rapid evolution of 6-phenylpurine inhibitors of protein kinase B through structure-based design.,Donald A, McHardy T, Rowlands MG, Hunter LJ, Davies TG, Berdini V, Boyle RG, Aherne GW, Garrett MD, Collins I J Med Chem. 2007 May 17;50(10):2289-92. Epub 2007 Apr 24. PMID:17451235[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Donald A, McHardy T, Rowlands MG, Hunter LJ, Davies TG, Berdini V, Boyle RG, Aherne GW, Garrett MD, Collins I. Rapid evolution of 6-phenylpurine inhibitors of protein kinase B through structure-based design. J Med Chem. 2007 May 17;50(10):2289-92. Epub 2007 Apr 24. PMID:17451235 doi:10.1021/jm0700924
