2OJQ

Crystal structure of Alix V domain

Summary for 2OJQ

• Entry DOI: 10.2210/pdb2ojq/pdb
• Descriptor: Programmed cell death 6-interacting protein (1 entity in total)
• Functional Keywords: helical, apoptosis
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytosol : Q8WUM4
• Total number of polymer chains: 1
• Total formula weight: 39193.41

Authors

Lee, S.,Hurley, J.H. (deposition date: 2007-01-13, release date: 2007-02-20, Last modification date: 2024-10-16)

Primary citation

Lee, S.,Joshi, A.,Nagashima, K.,Freed, E.O.,Hurley, J.H.
Structural basis for viral late-domain binding to Alix
Nat.Struct.Mol.Biol., 14:194-199, 2007

PubMed 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.

PubMed: 17277784
DOI: 10.1038/nsmb1203

Experimental method

X-RAY DIFFRACTION (2.87 Å)