Abstract
2,3,5-Trisubstituted pyridines have been designed as potent AKT inhibitors that are selective against ROCK1 based on the comparison between AKT and ROCK1 structures. Substitution at the 2-position of the core pyridine is the key element to provide selectivity against ROCK1. An X-ray co-crystal structure of 9p in PKA supports the proposed rationale of ROCK1 selectivity.
Copyright 2009 Elsevier Ltd. All rights reserved.
MeSH terms
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Binding Sites
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Crystallography, X-Ray
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Humans
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Protein Kinase Inhibitors / chemical synthesis
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Protein Kinase Inhibitors / chemistry*
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Protein Kinase Inhibitors / pharmacology
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Proto-Oncogene Proteins c-akt / antagonists & inhibitors*
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Proto-Oncogene Proteins c-akt / metabolism
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Pyridines / chemical synthesis
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Pyridines / chemistry*
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Pyridines / pharmacology
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Structure-Activity Relationship
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rho-Associated Kinases / antagonists & inhibitors*
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rho-Associated Kinases / metabolism
Substances
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Protein Kinase Inhibitors
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Pyridines
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Proto-Oncogene Proteins c-akt
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ROCK1 protein, human
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rho-Associated Kinases