2OEW

Structure of ALIX/AIP1 Bro1 Domain

Summary for 2OEW

• Entry DOI: 10.2210/pdb2oew/pdb
• Related: 2OEV 2OEX
• Descriptor: Programmed cell death 6-interacting protein (2 entities in total)
• Functional Keywords: tetratricopeptide repeat, tpr, protein transport
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytosol : Q8WUM4
• Total number of polymer chains: 1
• Total formula weight: 42735.79

Authors

Fisher, R.D.,Zhai, Q.,Robinson, H.,Hill, C.P. (deposition date: 2007-01-01, release date: 2007-03-27, Last modification date: 2023-08-30)

Primary citation

Fisher, R.D.,Chung, H.Y.,Zhai, Q.,Robinson, H.,Sundquist, W.I.,Hill, C.P.
Structural and Biochemical Studies of ALIX/AIP1 and Its Role in Retrovirus Budding
Cell(Cambridge,Mass.), 128:841-852, 2007

PubMed Abstract: 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.

PubMed: 17350572
DOI: 10.1016/j.cell.2007.01.035

Experimental method

X-RAY DIFFRACTION (2.55 Å)