Evaluation of the interaction between phosphohistidine analogues and phosphotyrosine binding domains.
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.
School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Woodhouse Lane, Leeds, LS2 9JT (UK) http://www.chem.leeds.ac.uk/MEW/
Tom E
TE
McAllister
Katherine A
KA
Horner
Michael E
ME
Webb
D001665:Binding Sites; D002151:Calorimetry; D005057:Eukaryotic Cells / Q000737:chemistry; D005454:Fluorescence Polarization; D051380:GRB2 Adaptor Protein / Q000737:chemistry*; D006639:Histidine / Q000031:analogs & derivatives* / Q000737:chemistry; D006801:Humans; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D019000:Phosphotyrosine / Q000737:chemistry*; D014230:Triazoles / Q000737:chemistry*; D018909:src Homology Domains
D051380:GRB2 Adaptor Protein; C495948:GRB2 protein, human; D010455:Peptides; D014230:Triazoles; D019000:Phosphotyrosine; D006639:Histidine; C005436:phosphohistidine
cell signaling; phosphohistidine; phosphotyrosine; protein modifications; synthetic analogues