Open AccessStructural studies of the catalytic core of the primate foamy virus (PFV‐1) integrase
Author(s) -
Réty Stéphane,
Řežábková Lenka,
Dubanchet Barbara,
Šilhán Jan,
Legrand Pierre,
LewitBentley Anita
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110022852
Subject(s) - integrase , integrases , enzyme , chemistry , catalysis , molecule , virology , crystallography , divalent , virus , human immunodeficiency virus (hiv) , stereochemistry , biology , biochemistry , organic chemistry
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.