2oex: Difference between revisions

Revision as of 06:39, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2oex.png

Template:STRUCTURE 2oex

Structure of ALIX/AIP1 V DomainStructure of ALIX/AIP1 V Domain

Template:ABSTRACT PUBMED 17350572

About this StructureAbout this Structure

2OEX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding., Fisher RD, Chung HY, Zhai Q, Robinson H, Sundquist WI, Hill CP, Cell. 2007 Mar 9;128(5):841-52. PMID:17350572

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OCA

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-'''Structure of ALIX/AIP1 V Domain'''
+===Structure of ALIX/AIP1 V Domain===
-==Overview==
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-ALIX/AIP1 functions in enveloped virus budding, endosomal protein sorting, and many other cellular processes. Retroviruses, including HIV-1, SIV, and EIAV, bind and recruit ALIX through YPX(n)L late-domain motifs (X = any residue; n = 1-3). Crystal structures reveal that human ALIX is composed of an N-terminal Bro1 domain and a central domain that is composed of two extended three-helix bundles that form elongated arms that fold back into a "V." The structures also reveal conformational flexibility in the arms that suggests that the V domain may act as a flexible hinge in response to ligand binding. YPX(n)L late domains bind in a conserved hydrophobic pocket on the second arm near the apex of the V, whereas CHMP4/ESCRT-III proteins bind a conserved hydrophobic patch on the Bro1 domain, and both interactions are required for virus budding. ALIX therefore serves as a flexible, extended scaffold that connects retroviral Gag proteins to ESCRT-III and other cellular-budding machinery.
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