Ontology type: schema:ScholarlyArticle
2005-08
AUTHORSFrançois Ternois, Jana Sticht, Stéphane Duquerroy, Hans-Georg Kräusslich, Félix A Rey
ABSTRACTImmature HIV particles bud from infected cells after assembly at the cytoplasmic side of cellular membranes. This assembly is driven by interactions between Gag polyproteins. Mature particles, each containing a characteristic conical core, are later generated by proteolytic maturation of Gag in the virion. The C-terminal domain of the HIV-1 capsid protein (C-CA) has been shown to contain oligomerization determinants essential for particle assembly. Here we report the 1.7-A-resolution crystal structure of C-CA in complex with a peptide capable of inhibiting immature- and mature-like particle assembly in vitro. The peptide inserts as an amphipathic alpha-helix into a conserved hydrophobic groove of C-CA, resulting in formation of a compact five-helix bundle with altered dimeric interactions. This structure thus reveals the details of an allosteric site in the HIV capsid protein that can be targeted for antiviral therapy. More... »
PAGES678-682
http://scigraph.springernature.com/pub.10.1038/nsmb967
DOIhttp://dx.doi.org/10.1038/nsmb967
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PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/16041386
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