화학공학소재연구정보센터
Journal of the American Chemical Society, Vol.118, No.45, 11265-11277, 1996
Structural Characterization of the Phosphotyrosine Binding Region of a High-Affinity Sh2 Domain-Phosphopeptide Complex by Molecular-Dynamics Simulation and Chemical-Shift Calculations
Three molecular dynamics simulations of the free, phosphate ion-bound and phosphopeptide-bound C-terminal SH2 domain of phospholipase C-gamma l (PLCC . pY) have been performed to aid in the interpretation of chemical shift data and the elucidation of interatomic interactions at the phosphotyrosine (pTyr) binding region. The simulation of the phosphopeptide complex was carried out with newly developed CHARMM force-field parameters for pTyr, optimized against experimental data and ab initio calculations. The lack of NOEs involving phosphate in the binding pocket had necessitated a chemical shift analysis of the pTyr binding region for a more detailed characterization of the hydrogen bonding interactions involving pTyr.