2ojq
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(New page: 200px<br /> <applet load="2ojq" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ojq, resolution 2.87Å" /> '''Crystal structure o...)
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Revision as of 21:05, 12 November 2007
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Crystal structure of Alix V domain
Overview
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.
About this Structure
2OJQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for viral late-domain binding to Alix., Lee S, Joshi A, Nagashima K, Freed EO, Hurley JH, Nat Struct Mol Biol. 2007 Mar;14(3):194-9. Epub 2007 Feb 4. PMID:17277784
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