2oew
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Structure of ALIX/AIP1 Bro1 Domain
OverviewOverview
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.
About this StructureAbout this Structure
2OEW 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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