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Updated: Jun 2, 2026

Modeling an Enzyme Active Site using Molecular Visualization Freeware
Published on: December 25, 2021
From structure--based to knowledge--based drug design through x-ray protein crystallography: sketching glycogen
E D Chrysina1, A Chajistamatiou, M Chegkazi
1Institute of Organic and Pharmaceutical Chemistry, National Hellenic Research Foundation, 48, Vassileos Constantinou Avenue, GR-11635 Athens, Greece. echrysina@eie.gr
Abstract:
The knowledge derived from the three-dimensional structure of a macromolecular receptor either in the native form or in complex with different ligands has given new insights to the development of improved drug candidates contributing to the drug development pipeline. The structure-based drug design approach has been tested on a number of macromolecular targets implicated in various diseases such as hypertension, glaucoma, HIV and influenza. This approach has also been employed for the development of new antidiabetic agents targeting glycogen phosphorylase (GP), an enzyme that modulates glucose levels in blood circulation. The key role of x-ray protein crystallography in the structure-based inhibitor design process is presented by the case of rabbit muscle GP (RMGPb) that shares increased homology with the liver isoenzyme. The properties of the allosteric binding sites of RMGPb are revealed by filing the interactions formed upon binding of characteristic functional groups and documenting the changes induced in the residues lining the site of interest.
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