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Evaluation of the Interaction between Phosphohistidine Analogues and Phosphotyrosine Binding Domains
Author(s) -
McAllister Tom E.,
Horner Katherine A.,
Webb Michael E.
Publication year - 2014
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201402090
Subject(s) - isothermal titration calorimetry , chemistry , biochemistry , protein–protein interaction , grb2 , sh2 domain , peptide , phosphorylation , signal transducing adaptor protein , tyrosine phosphorylation
We have investigated the interaction of peptides containing phosphohistidine analogues and their homologues with the prototypical phosphotyrosine binding SH2 domain from the eukaryotic cell signalling protein Grb2 by using a combination of isothermal titration calorimetry and a fluorescence anisotropy competition assay. These investigations demonstrated that the triazole class of phosphohistidine analogues are capable of binding too, suggesting that phosphohistidine could potentially be detected by this class of proteins in vivo.