Structural studies of the catalytic core of the primate foamy virus (PFV-1) integrase.
Retroviral integrases are vital enzymes in the viral life cycle and thus are important targets for antiretroviral drugs. The structure of the catalytic core domain of the integrase from human foamy virus, which is related to HIV-1, has been solved. The structure of the protein is presented in two different crystal forms, each containing several molecules in the asymmetric unit, with and without the essential manganese or magnesium ion, and the structures are compared in detail. This allows regions of high structural variability to be pinpointed, as well as the effect of divalent cations on the conformation of the catalytic site.
Réty
Stéphane
S
Laboratoire de Biologie et Pharmacologie Appliquée, CNRS UMR8113, Ecole Normale Supérieure de Cachan, 61 Avenue du Président Wilson, 94235 Cachan, France. stephane.rety@parisdescartes.fr
Reaeábková
Lenka
L
Dubanchet
Barbara
B
Silhán
Jan
J
Legrand
Pierre
P
Lewit-Bentley
Anita
A
D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D019426:Integrases / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D009154:Mutation; D017434:Protein Structure, Tertiary; D016092:Spumavirus / Q000201:enzymology*; D040681:Structural Homology, Protein
D019426:Integrases