4.5 Article

Structural basis for viral late-domain binding to Alix

Journal

NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 14, Issue 3, Pages 194-199

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1203

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Funding

  1. Intramural NIH HHS [Z01 DK036118-14] Funding Source: Medline
  2. NCI NIH HHS [N01CO12400, N01-CO-12400] Funding Source: Medline

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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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