Evaluation of the Interaction between Phosphohistidine Analogues and Phosphotyrosine Binding Domains
Article first published online: 25 APR 2014
© 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.
Volume 15, Issue 8, pages 1088–1091, May 26, 2014
How to Cite
McAllister, T. E., Horner, K. A. and Webb, M. E. (2014), Evaluation of the Interaction between Phosphohistidine Analogues and Phosphotyrosine Binding Domains. ChemBioChem, 15: 1088–1091. doi: 10.1002/cbic.201402090
- Issue published online: 21 MAY 2014
- Article first published online: 25 APR 2014
- Manuscript Received: 13 MAR 2014
- Funded Access
- EPSRC. Grant Number: EP/I013083/1
- cell signaling;
- protein modifications;
- synthetic analogues
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.