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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 anisotro...

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Detalles Bibliográficos
Autores principales: McAllister, Tom E, Horner, Katherine A, Webb, Michael E
Formato: Online Artículo Texto
Lenguaje:English
Publicado: WILEY-VCH Verlag 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4159583/
https://www.ncbi.nlm.nih.gov/pubmed/24771713
http://dx.doi.org/10.1002/cbic.201402090
Descripción
Sumario: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.