molecular docking of short chain glycosaminoglycan ligands in 3d model of bovine testicular hyaluronidase
2018
1. Abstract Computational analysis of
molecular docking of 3D model of bovine testicular hyaluronidase in silico
with a trimer (hexasaccharide) chondroitin sulfate and tetramer (octasaccharide)
heparin has demonstrated eight significant binding sites (cs1-cs8) for these
ligands. Interactions with heparin that inactivates the enzyme and protective
effects of chondroitin sulfate were examined. Binding sites have been
identified which are critical for stabilization of the protein structure after
chondroitin sulfate binding: at positions cs2, cs4, cs7 and cs8 or cs1, cs2,
cs4, cs7 and cs8. Occupation of these sites is theoretically sufficient for
prevention of irreversible molecular deformations after heparin inclusion into
active site. The presence of sensitivity
sites on hyaluronidase globule indicates the possibility of regulating the
enzyme function via coupling glycosaminoglycan ligands thus initiating delicate/fine
formation of effective electrostatic potential.
Interactions between glycosaminoglycan ligands and hyaluronidase are
based primarily on electrostatic forces. 2. Keywords: Bovine Testicular Hyaluronidase; Chondroitin Sulfate; Docking; Glycosaminoglycan
Ligands; Heparin
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