Abstract
Optimization of kinase selectivity for a set of benzothiophene MK2 inhibitors provided analogs with potencies of less than 500 nM in a cell based assay. The selectivity of the inhibitors can be rationalized by examination of X-ray crystal structures of inhibitors bound to MK2.
MeSH terms
-
Binding Sites
-
Cell Line, Tumor
-
Crystallography, X-Ray
-
Cyclin-Dependent Kinase 2 / antagonists & inhibitors
-
Cyclin-Dependent Kinase 2 / metabolism
-
Drug Design
-
Humans
-
MAP Kinase Kinase 2 / antagonists & inhibitors*
-
MAP Kinase Kinase 2 / metabolism
-
Protein Kinase Inhibitors / chemical synthesis
-
Protein Kinase Inhibitors / chemistry*
-
Protein Kinase Inhibitors / pharmacology
-
Thiophenes / chemical synthesis
-
Thiophenes / chemistry*
-
Thiophenes / pharmacology
Substances
-
Protein Kinase Inhibitors
-
Thiophenes
-
benzothiophene
-
Cyclin-Dependent Kinase 2
-
MAP Kinase Kinase 2