Abstract
We have determined the structure of an Shc-derivedphosphotyrosine-containing peptide complexed with Grb2 SH2 based on intra-and intermolecular NOE correlations observed by a series of isotope-filteredNMR experiments using a PFG z-filter. In contrast to an extendedconformation of phosphotyrosine-containing peptides bound to Src, Syp andPLC γ SH2s, the Shc-derived peptide formed a turn at the +1 and +2positions next to the phosphotyrosine residue. Trp121, locatedat the EF1 site of Grb2 SH2, blocked the peptide binding in an extendedconformation. The present study confirms that eachphosphotyrosine-containing peptide binds to the cognate SH2 with a specificconformation, which gives the structural basis for the binding specificitybetween SH2s and target proteins.
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Ogura, K., Tsuchiya, S., Terasawa, H. et al. Conformation of an Shc-derived phosphotyrosine-containing peptide complexed with the Grb2 SH2 domain. J Biomol NMR 10, 273–278 (1997). https://doi.org/10.1023/A:1018340506337
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DOI: https://doi.org/10.1023/A:1018340506337