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Cyplecksins Are Covalent Inhibitors of the Pleckstrin Homology Domain of Cytohesin
Author(s) -
Hussein Mohamed,
Bettio Martina,
Schmitz Anton,
Hannam Jeffrey S.,
Theis Julian,
Mayer Günter,
Dosa Stefan,
Gütschow Michael,
Famulok Michael
Publication year - 2013
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.201302207
Subject(s) - pleckstrin homology domain , guanine nucleotide exchange factor , gtpase , covalent bond , microbiology and biotechnology , chemistry , function (biology) , dock , biochemistry , computational biology , biology , membrane , organic chemistry
The covalent grip : A new class of 5‐bromobarbiturates (Cyplecksins; see structure) act by a covalent mechanism to inhibit the biological function of the pleckstrin homology domain of cytohesins, small guanine nucleotide exchange factors for the Ras‐like ARF‐GTPases. In cells, Cyplecksins interfere with the phosphoinositol‐dependent membrane recruitment of cytohesins. Cyplecksins may be useful in validating cytohesins as potential drug targets.