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Fraternali, F ; Do, QT ; Doan, BT ; Atkinson, RA ; Palmas, P ; Sklenar, V ; Safar, P ; Wildgoose, P ; Strop, P ; Saudek, V

Mapping the active site of factor Xa by selective inhibitors : An NMR and MD study

Proteins-Structure Function and Genetics 30 (3) 264-274

par Administrateur - publié le

Abstract :

The structure of two selective inhibitors, Ac-Tyr-Ile-Arg-Ile-Pro-NH2 and Ac-(4-Amino-Phe)-(Cyclohexyl-Gly)-Arg-NH2, in the active site of the blood clotting enzyme factor Zia was determined by using transferred nuclear Overhauser effect nuclear magnetic resonance (NMR) spectroscopy, They represent a family of peptidic inhibitors obtained by the screening of a vast combinatorial library. Each structure was first calculated by using standard computational procedures (distance geometry, simulated annealing, energy minimization) and then further refined by systematic search of the conformation of the inhibitor docked in the active site and repeating the simulated annealing and energy minimization.