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Structural basis for viral late-domain binding to Alix

  1. Author:
    Lee, S.
    Joshi, A.
    Nagashima, K.
    Freed, E. O.
    Hurley, J. H.

  2. Author Address

    NIDDK, Mol Biol Lab, NIH, US Dept Htlh & Human Serv, Bethesda, MD 20892 USA. NCI, Virus Cell Interact Sect, HIV Drug Resistance Program, NIH,US Dept Htlh & Human Serv, Frederick, MD 21702 USA. NCI, Image Anal Lab, Res Technol Program, SAIC Frederick,NIH,US Dept Hlth & Human Serv, Frederick, MD 21702 USA.;Hurley, JH, NIDDK, Mol Biol Lab, NIH, US Dept Htlh & Human Serv, Bethesda, MD 20892 USA.;hurley@helix.nih.gov
    1. Year: 2007
    2. Date: Mar
  2. Journal: Nature Structural & Molecular Biology
    1. 14
    2. 3
    3. Pages: 194-199
  4. Type of Article: Article
  5. ISSN: 1545-9985
  1. Abstract:

    The modular protein Alix is a central node in endosomal-lysosomal trafficking and the budding of human immunodeficiency virus (HIV)-1. The Gag p6 protein of HIV-1 contains a LYPx(n)LxxL motif that is required for Alix-mediated budding and binds a region of Alix spanning residues 360-702. The structure of this fragment of Alix has the shape of the letter 'V' and is termed the V domain. The V domain has a topologically complex arrangement of 11 alpha-helices, with connecting loops that cross three times between the two arms of the V. The conserved residue Phe676 is at the center of a large hydrophobic pocket and is crucial for binding to a peptide model of HIV-1 p6. Overexpression of the V domain inhibits HIV-1 release from cells. This inhibition of release is reversed by mutations that block binding of the Alix V domain to p6.

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  2. DOI: 10.1038/nsmb1203
  3. View record in Web of Science®
  4. WOS: 000244715200007

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