Investigation on the sucrose binding pocket of HIV-1 Integrase by molecular dynamics and synergy experiments.
Bioorg Med Chem Lett
; 25(15): 3013-6, 2015 Aug 01.
Article
en En
| MEDLINE
| ID: mdl-26048795
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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Sacarosa
/
VIH-1
/
Inhibidores de Integrasa VIH
/
Integrasa de VIH
Límite:
Humans
Idioma:
En
Revista:
Bioorg Med Chem Lett
Asunto de la revista:
BIOQUIMICA
/
QUIMICA
Año:
2015
Tipo del documento:
Article
País de afiliación:
Italia