The C-terminal domain of the HIV-1 regulatory protein Vpr adopts an antiparallel dimeric structure in solution via its leucine-zipper-like domain.

ABSTRACT: HIV-1 Vpr is a highly conserved accessory protein that is involved in many functions of the virus life cycle. Vpr facilitates the entry of the HIV pre-integration complex through the nuclear pore, induces G2 cell cycle arrest, regulates cell apoptosis, increases transcription from the long terminal repeat and enhances viral replication. Vpr contains a Leu/Ile-rich domain (amino acids 60-81) in its C-terminal part, which is critical for dimerization. The sequence comprising residues 52-96 is implicated in properties of the protein such as DNA interaction and apoptosis via interaction with the adenine nucleotide translocator. To understand the specific interactions of Vpr-(52-96), the ability of this peptide to dimerize via a leucine-zipper mechanism has been investigated, by NMR and fluores

SUBMITTER: Bourbigot S 

PROVIDER: S-EPMC1134961 | biostudies-literature | 2005 Apr

REPOSITORIES: biostudies-literature