The HIV-1 capsid protein C-terminal domain in complex with a virus assembly inhibitor View Full Text


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Article Info

DATE

2005-08

AUTHORS

François Ternois, Jana Sticht, Stéphane Duquerroy, Hans-Georg Kräusslich, Félix A Rey

ABSTRACT

Immature 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... »

PAGES

678-682

References to SciGraph publications

  • 2005-08. A peptide inhibitor of HIV-1 assembly in vitro in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2000-09. Image reconstructions of helical assemblies of the HIV-1 CA protein in NATURE
  • 1996-09. Crystal structure of dimeric HIV-1 capsid protein in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2004-07. The stoichiometry of Gag protein in HIV-1 in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2002-05-28. Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nsmb967

    DOI

    http://dx.doi.org/10.1038/nsmb967

    DIMENSIONS

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    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/16041386


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