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Evaluation of the interaction between phosphohistidine analogues and phosphotyrosine binding domains.

ABSTRACT: 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.

SUBMITTER: McAllister TE

PROVIDER: S-EPMC4159583 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature

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Evaluation of the interaction between phosphohistidine analogues and phosphotyrosine binding domains.

McAllister Tom E TE Horner Katherine A KA Webb Michael E ME

Chembiochem : a European journal of chemical biology 20140425 8

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 ...[more]

PMID: 24771713

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