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Redox‐Based Probes for Protein Tyrosine Phosphatases
Author(s) -
Leonard Stephen E.,
Garcia Francisco J.,
Goodsell David S.,
Carroll Kate S.
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201007871
Subject(s) - protein tyrosine phosphatase , tyrosine , redox , biochemistry , chemistry , cysteine , computational biology , phosphatase , active site , identification (biology) , adduct , computer science , combinatorial chemistry , enzyme , biology , organic chemistry , botany
Three in one : The design strategy for redox‐based probes (RBPs) that detect the reversible oxidation of protein tyrosine phosphatases (PTPs) includes a “warhead” that forms a covalent adduct with the oxidized active site cysteine of PTPs, a synthetic module that directs binding to the PTP active site, and a chemical reporter tag used for the identification, purification, or direct visualization of the probe‐labeled proteins (see picture).