Abstract
Going against tradition: although most kinase inhibitors are ATP competitive, lariat peptides inhibit Abl kinase activity in an ATP-uncompetitive manner. Further, lariat peptides discriminated Src family kinases, and recognize the allosteric region that lies adjacent to the ATP binding pocket in the Abl kinase catalytic cleft.
Keywords:
Abl kinase; combinatorial chemistry; enzyme inhibitors; lariat peptides; uncompetitive inhibition.
Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Adenosine Triphosphate / chemistry
-
Adenosine Triphosphate / metabolism
-
Allosteric Regulation
-
Amino Acid Sequence
-
Binding Sites
-
Catalytic Domain
-
Cell Line, Tumor
-
Enzyme Activation / drug effects
-
Humans
-
Kinetics
-
Peptides / chemistry
-
Peptides / metabolism*
-
Peptides / pharmacology*
-
Protein Binding
-
Protein Kinase Inhibitors / chemistry
-
Protein Kinase Inhibitors / metabolism
-
Protein Kinase Inhibitors / pharmacology
-
Proto-Oncogene Proteins c-abl / antagonists & inhibitors*
-
Proto-Oncogene Proteins c-abl / metabolism
Substances
-
Peptides
-
Protein Kinase Inhibitors
-
Adenosine Triphosphate
-
Proto-Oncogene Proteins c-abl