3R9M

Crystal structure of the Brox Bro1 domain

3R9M の概要

• エントリーDOI: 10.2210/pdb3r9m/pdb
• 関連するPDBエントリー: 3RAU
• 分子名称: BRO1 domain-containing protein BROX, 1,2-ETHANEDIOL, FORMIC ACID, ... (4 entities in total)
• 機能のキーワード: bro1 domain, protein binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Lipid-anchor (Potential): Q5VW32
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43464.06

構造登録者

Mu, R.L.,Jiang, J.S.,Snyder, G.,Smith, P.,Xiao, T. (登録日: 2011-03-25, 公開日: 2011-09-14, 最終更新日: 2023-09-13)

主引用文献

Sette, P.,Mu, R.,Dussupt, V.,Jiang, J.,Snyder, G.,Smith, P.,Xiao, T.S.,Bouamr, F.
The Phe105 Loop of Alix Bro1 Domain Plays a Key Role in HIV-1 Release.
Structure, 19:1485-1495, 2011

PubMed Abstract: Alix and cellular paralogs HD-PTP and Brox contain N-terminal Bro1 domains that bind ESCRT-III CHMP4. In contrast to HD-PTP and Brox, expression of the Bro1 domain of Alix alleviates HIV-1 release defects that result from interrupted access to ESCRT. In an attempt to elucidate this functional discrepancy, we solved the crystal structures of the Bro1 domains of HD-PTP and Brox. They revealed typical "boomerang" folds they share with the Bro1 Alix domain. However, they each contain unique structural features that may be relevant to their specific function(s). In particular, phenylalanine residue in position 105 (Phe105) of Alix belongs to a long loop that is unique to its Bro1 domain. Concurrently, mutation of Phe105 and surrounding residues at the tip of the loop compromise the function of Alix in HIV-1 budding without affecting its interactions with Gag or CHMP4. These studies identify a new functional determinant in the Bro1 domain of Alix.

PubMed: 21889351
DOI: 10.1016/j.str.2011.07.016

実験手法

X-RAY DIFFRACTION (1.95 Å)