Calorimetric and structural studies of 1,2,3-trisubstituted cyclopropanes as conformationally constrained peptide inhibitors of Src SH2 domain binding.

Abstract

Isothermal titration calorimetry and X-ray crystallography have been used to determine the structural and thermodynamic consequences associated with constraining the pTyr residue of the pYEEI ligand for the Src Homology 2 domain of the Src kinase (Src SH2 domain). The conformationally constrained peptide mimics that were used are cyclopropane-derived… (More)

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Cite this paper

@article{Davidson2002CalorimetricAS, title={Calorimetric and structural studies of 1,2,3-trisubstituted cyclopropanes as conformationally constrained peptide inhibitors of Src SH2 domain binding.}, author={James Patrick Davidson and Olga Y Lubman and Thierry Rose and Gabriel Waksman and Stephen F Martin}, journal={Journal of the American Chemical Society}, year={2002}, volume={124 2}, pages={205-15} }