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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
WILEY-VCH Verlag
2014
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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. |
format | Online Article Text |
id | pubmed-4159583 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | WILEY-VCH Verlag |
record_format | MEDLINE/PubMed |
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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