Ontology highlight
ABSTRACT:
SUBMITTER: Chio CM
PROVIDER: S-EPMC4554683 | biostudies-literature | 2015 Aug
REPOSITORIES: biostudies-literature
Chio Cynthia M CM Cheng Karen W KW Bishop Anthony C AC
Chembiochem : a European journal of chemical biology 20150630 12
Few chemical strategies for activating enzymes have been developed. Here we show that a biarsenical compound (FlAsH) can directly activate a rationally engineered protein tyrosine phosphatase (Shp2 PTP) by disrupting autoinhibitory interactions between Shp2's N-terminal SH2 domain and its PTP domain. We found that introducing a tricysteine motif at a loop of Shp2's N-SH2 domain confers affinity for FlAsH; binding of FlAsH to the cysteine-enriched loop relieves Shp2's inhibitory interdomain inter ...[more]