2UWQ

Solution structure of ASPP2 N-terminus

2UWQ の概要

• エントリーDOI: 10.2210/pdb2uwq/pdb
• 関連するPDBエントリー: 1YCS
• 分子名称: APOPTOSIS-STIMULATING OF P53 PROTEIN 2 (1 entity in total)
• 機能のキーワード: aspp2, ubiquitin-like, sh3-domain, apoptosis, cell cycle, ank repeat, sh3-binding
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasm, perinuclear region: Q13625
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9976.22

構造登録者

Tidow, H.,Rutherford, T.J.,Andreeva, A.,Fersht, A.R. (登録日: 2007-03-22, 公開日: 2007-07-10, 最終更新日: 2024-05-15)

主引用文献

Tidow, H.,Andreeva, A.,Rutherford, T.J.,Fersht, A.R.
Solution structure of ASPP2 N-terminal domain (N-ASPP2) reveals a ubiquitin-like fold.
J. Mol. Biol., 371:948-958, 2007

PubMed Abstract: Proteins of the ASPP family bind to p53 and regulate p53-mediated apoptosis. Two family members, ASPP1 and ASPP2, have pro-apoptotic functions while iASPP shows anti-apoptotic responses. However, both the mechanism of enhancement/repression of apoptosis and the molecular basis for their different responses remain unknown. To address the role of the N-termini of pro-apoptotic ASPP proteins, we solved the solution structure of N-ASPP2 (1-83) by NMR spectroscopy. The structure of this domain reveals a beta-Grasp ubiquitin-like fold. Our findings suggest a possible role for the N-termini of ASPP proteins in binding to other proteins in the apoptotic response network and thus mediating their selective pro-apoptotic function.

PubMed: 17594908
DOI: 10.1016/j.jmb.2007.05.024

実験手法

SOLUTION NMR