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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
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author McAllister, Tom E
Horner, Katherine A
Webb, Michael E
author_facet McAllister, Tom E
Horner, Katherine A
Webb, Michael E
author_sort McAllister, Tom E
collection PubMed
description 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.
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spelling pubmed-41595832014-09-22 Evaluation of the Interaction between Phosphohistidine Analogues and Phosphotyrosine Binding Domains McAllister, Tom E Horner, Katherine A Webb, Michael E Chembiochem Communications 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. WILEY-VCH Verlag 2014-05-26 2014-04-25 /pmc/articles/PMC4159583/ /pubmed/24771713 http://dx.doi.org/10.1002/cbic.201402090 Text en © 2014 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. https://creativecommons.org/licenses/by/4.0/ © 2014 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Communications
McAllister, Tom E
Horner, Katherine A
Webb, Michael E
Evaluation of the Interaction between Phosphohistidine Analogues and Phosphotyrosine Binding Domains
title Evaluation of the Interaction between Phosphohistidine Analogues and Phosphotyrosine Binding Domains
title_full Evaluation of the Interaction between Phosphohistidine Analogues and Phosphotyrosine Binding Domains
title_fullStr Evaluation of the Interaction between Phosphohistidine Analogues and Phosphotyrosine Binding Domains
title_full_unstemmed Evaluation of the Interaction between Phosphohistidine Analogues and Phosphotyrosine Binding Domains
title_short Evaluation of the Interaction between Phosphohistidine Analogues and Phosphotyrosine Binding Domains
title_sort evaluation of the interaction between phosphohistidine analogues and phosphotyrosine binding domains
topic Communications
url 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
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