Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1370711 | Bioorganic & Medicinal Chemistry Letters | 2015 | 4 Pages |
Abstract
Enzymes whose catalytic activity depends on multimeric assembly are targets for inhibitors that perturb the interactions between the protein subunits such as the HIV-1 Integrase (IN). Sucrose has been recently crystallized in complex with IN revealing an allosteric binding pocket at the monomer–monomer interface. Herein, molecular dynamics were applied to theoretically test the effect of this small ligand on IN. As a result, such a compound increases the mutual free energy of binding between the two interacting monomers. Biological experiments confirmed the computational forecast.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slide
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Cristina Tintori, Francesca Esposito, Francesca Morreale, Riccardo Martini, Enzo Tramontano, Maurizio Botta,