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A. V. Maksimenko, R. S. Beabealashvili
Electrostatic
interactions for docking bovine testicular hyaluronidase 3D-model with
chondroitin sulfate trimers and heparin tetramers
Abstract
Molecular
docking 3D-model of bovine testicular hyaluronidase with glycosaminoglycan
ligands was performed. Chondroitin sulfate trimer and heparin tetramer were used
as ligands. Methods of computational chemistry were applied for elucidation of
hyaluronidase functioning regulation, when heparin ligand inactivated
biocatalyst and chondroitin sulfate ligand protected the enzyme structure. The
eight binding sites on enzyme molecular surface were determined for
glycosaminoglycan ligand coupling due to electrostatic interactions. Herewith
there is the possibility for reversible and irreversible conformational
alterations of 3D-model of enzyme. Suffusion of critical binding sites of
hyaluronidase is sufficed for prevention of irreversible deformations of enzyme
active site cave. The interaction of glycosaminoglycan ligands with
hyaluronidase is determined by electrostatic forces mainly.
Key words:
bovine testicular hyaluronidase, tertiary structure, glycosaminoglycan ligand,
electrostatic interactions, docking, chondroitin sulfate, heparin, surface
electrostatic enzyme potential, enzyme functioning regulation.
Copyright (C) Chemistry Dept., Moscow State University, 2002
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