2R03

Crystal Structure of ALIX/AIP1 in complex with the YPDL Late Domain

2R03 の概要

• エントリーDOI: 10.2210/pdb2r03/pdb
• 関連するPDBエントリー: 2R02 2R05
• 分子名称: Programmed cell death 6-interacting protein, p6-Gag (3 entities in total)
• 機能のキーワード: coiled-coil, apoptosis, cytoplasm, host-virus interaction, polymorphism, protein transport, transport, capsid protein, core protein, metal-binding, virion, zinc, zinc-finger
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm, cytosol : Q8WUM4; Virion : P69732
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79024.67

構造登録者

Hill, C.P.,Zhai, Q.,Fisher, R.D. (登録日: 2007-08-17, 公開日: 2007-12-18, 最終更新日: 2024-02-21)

主引用文献

Zhai, Q.,Fisher, R.D.,Chung, H.Y.,Myszka, D.G.,Sundquist, W.I.,Hill, C.P.
Structural and functional studies of ALIX interactions with YPX(n)L late domains of HIV-1 and EIAV.
Nat.Struct.Mol.Biol., 15:43-49, 2008

PubMed Abstract: Retrovirus budding requires short peptide motifs (late domains) located within the viral Gag protein that function by recruiting cellular factors. The YPX(n)L late domains of HIV and other lentiviruses recruit the protein ALIX (also known as AIP1), which also functions in vesicle formation at the multivesicular body and in the abscission stage of cytokinesis. Here, we report the crystal structures of ALIX in complex with the YPX(n)L late domains from HIV-1 and EIAV. The two distinct late domains bind at the same site on the ALIX V domain but adopt different conformations that allow them to make equivalent contacts. Binding studies and functional assays verified the importance of key interface residues and revealed that binding affinities are tuned by context-dependent effects. These results reveal how YPX(n)L late domains recruit ALIX to facilitate virus budding and how ALIX can bind YPX(n)L sequences with both n = 1 and n = 3.

PubMed: 18066081
DOI: 10.1038/nsmb1319

実験手法

X-RAY DIFFRACTION (2.59 Å)