Probing the target-specific inhibition of sensitized protein tyrosine phosphatases with biarsenical probes.

ABSTRACT: Selective control of enzyme activity is critical for elucidating the roles of specific proteins in signaling pathways. One potential means for developing truly target-specific inhibitors involves the use of protein engineering to sensitize a target enzyme to inhibition by a small molecule that does not inhibit homologous wild-type enzymes. Previously, it has been shown that protein tyrosine phosphatases (PTPs) can be sensitized to inhibition by a biarsenical probe, FlAsH-EDT2, which inhibits PTP activity by specifically binding to cysteine residues that have been introduced into catalytically important regions. In the present study, we developed an array of biarsenical probes, some newly synthesized and some previously reported, to investigate for the first time the structure-activity rela

SUBMITTER: Pomorski A 

PROVIDER: S-EPMC4303503 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature