Biochemical and virological analysis of the 18-residue C-terminal tail of HIV-1 integrase.

ABSTRACT:

Background

The 18 residue tail abutting the SH3 fold that comprises the heart of the C-terminal domain is the only part of HIV-1 integrase yet to be visualized by structural biology. To ascertain the role of the tail region in integrase function and HIV-1 replication, a set of deletion mutants that successively lacked three amino acids was constructed and analyzed in a variety of biochemical and virus infection assays. HIV-1/2 chimers, which harbored the analogous 23-mer HIV-2 tail in place of the HIV-1 sequence, were also studied. Because integrase mutations can affect steps in the replication cycle other than integration, defective mutant viruses were tested for integrase protein content and reverse transcription in addition to integration. The F185K core domain mutation, which i

SUBMITTER: Dar MJ 

PROVIDER: S-EPMC2770994 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature