Three new structures of the core domain of HIV-1 integrase: an active site that binds magnesium.

ABSTRACT: HIV-1 integrase is an essential enzyme in the life cycle of the virus, responsible for catalyzing the insertion of the viral genome into the host cell chromosome; it provides an attractive target for antiviral drug design. The previously reported crystal structure of the HIV-1 integrase core domain revealed that this domain belongs to the superfamily of polynucleotidyltransferases. However, the position of the conserved catalytic carboxylic acids differed from those observed in other enzymes of the class, and attempts to crystallize in the presence of the cofactor, Mg2+, were unsuccessful. We report here three additional crystal structures of the core domain of HIV-1 integrase mutants, crystallized in the presence and absence of cacodylate, as well as complexed with Mg2+. These three cryst

SUBMITTER: Goldgur Y 

PROVIDER: S-EPMC21307 | biostudies-literature | 1998 Aug

REPOSITORIES: biostudies-literature