Journal
JOURNAL OF CHEMICAL INFORMATION AND MODELING
Volume 51, Issue 6, Pages 1199-1204Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ci200153c
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This work addresses the link between selectivity and an unusual, folded conformation for the P-loop observed initially for MAP4K4 and subsequently for other kinases. Statistical and computational analyses of our crystal structure database demonstrate that inhibitors that induce the P-loop folded conformation tend to be more selective, especially if they take advantage of this specific conformation by interacting more favorably with a conserved Tyr or Phe residue from the P-loop.
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