1KPP

Structure of the Tsg101 UEV domain

1KPP の概要

• エントリーDOI: 10.2210/pdb1kpp/pdb
• 関連するPDBエントリー: 1KPQ
• 分子名称: Tumor susceptibility gene 101 protein (1 entity in total)
• 機能のキーワード: e2 fold, cell cycle
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q99816
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16633.35

構造登録者

Pornillos, O.,Alam, S.L.,Rich, R.L.,Myszka, D.G.,Davis, D.R.,Sundquist, W.I. (登録日: 2002-01-02, 公開日: 2002-05-24, 最終更新日: 2024-05-22)

主引用文献

Pornillos, O.,Alam, S.L.,Rich, R.L.,Myszka, D.G.,Davis, D.R.,Sundquist, W.I.
Structure and functional interactions of the Tsg101 UEV domain.
EMBO J., 21:2397-2406, 2002

PubMed Abstract: Human Tsg101 plays key roles in HIV budding and in cellular vacuolar protein sorting (VPS). In performing these functions, Tsg101 binds both ubiquitin (Ub) and the PTAP tetrapeptide 'late domain' motif located within the viral Gag protein. These interactions are mediated by the N-terminal domain of Tsg101, which belongs to the catalytically inactive ubiquitin E2 variant (UEV) family. We now report the structure of Tsg101 UEV and chemical shift mapping of the Ub and PTAP binding sites. Tsg101 UEV resembles canonical E2 ubiquitin conjugating enzymes, but has an additional N-terminal helix, an extended beta-hairpin that links strands 1 and 2, and lacks the two C-terminal helices normally found in E2 enzymes. PTAP-containing peptides bind in a hydrophobic cleft exposed by the absence of the C-terminal helices, whereas ubiquitin binds in a novel site surrounding the beta-hairpin. These studies provide a structural framework for understanding how Tsg101 mediates the protein-protein interactions required for HIV budding and VPS.

PubMed: 12006492
DOI: 10.1093/emboj/21.10.2397

実験手法

SOLUTION NMR