A possible role for the asymmetric C-terminal domain dimer of Rous sarcoma virus integrase in viral DNA binding.

ABSTRACT: Integration of the retrovirus linear DNA genome into the host chromosome is an essential step in the viral replication cycle, and is catalyzed by the viral integrase (IN). Evidence suggests that IN functions as a dimer that cleaves a dinucleotide from the 3' DNA blunt ends while a dimer of dimers (tetramer) promotes concerted integration of the two processed ends into opposite strands of a target DNA. However, it remains unclear why a dimer rather than a monomer of IN is required for the insertion of each recessed DNA end. To help address this question, we have analyzed crystal structures of the Rous sarcoma virus (RSV) IN mutants complete with all three structural domains as well as its two-domain fragment in a new crystal form at an improved resolution. Combined with earlier structural s

SUBMITTER: Shi K 

PROVIDER: S-EPMC3579926 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature