McAllister, TE, Horner, KA and Webb, ME (2014) Evaluation of the interaction between phosphohistidine analogues and phosphotyrosine binding domains. Chembiochem, 15 (8). 1088 - 1091. ISSN 1439-4227
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | (c) 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. |
Keywords: | cell signaling; phosphohistidine; phosphotyrosine; protein modifications; synthetic analogues; Binding Sites; Calorimetry; Eukaryotic Cells; Fluorescence Polarization; GRB2 Adaptor Protein; Histidine; Humans; Molecular Conformation; Peptides; Phosphotyrosine; Triazoles; src Homology Domains |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Chemistry (Leeds) > Organic Chemistry (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 13 Aug 2015 13:28 |
Last Modified: | 13 Aug 2015 13:28 |
Published Version: | http://dx.doi.org/10.1002/cbic.201402090 |
Status: | Published |
Publisher: | Wiley-VCH |
Identification Number: | 10.1002/cbic.201402090 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:85559 |