2Y6W

Structure of a Bcl-w dimer

2Y6W の概要

• エントリーDOI: 10.2210/pdb2y6w/pdb
• 関連するPDBエントリー: 1MK3 1O0L 1ZY3
• 分子名称: BCL-2-LIKE PROTEIN 2, DI(HYDROXYETHYL)ETHER, TRIETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: apoptosis
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Mitochondrion membrane; Peripheral membrane protein: Q92843
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39692.16

構造登録者

Lee, E.F.,Evangelista, M.,Pettikiriarachchi, A.,Dogovski, C.,Perugini, M.A.,Colman, P.M.,Fairlie, W.D. (登録日: 2011-01-27, 公開日: 2011-10-26, 最終更新日: 2023-12-20)

主引用文献

Lee, E.F.,Dewson, G.,Smith, B.J.,Evangelista, M.,Pettikiriarachchi, A.,Dogovski, C.,Perugini, M.A.,Colman, P.M.,Fairlie, W.D.
Crystal Structure of a Bcl-W Domain-Swapped Dimer: Implications for the Function of Bcl-2 Family Proteins.
Structure, 19:1467-, 2011

PubMed Abstract: The prosurvival and proapoptotic proteins of the BCL-2 family share a similar three-dimensional fold despite their opposing functions. However, many biochemical studies highlight the requirement for conformational changes for the functioning of both types of proteins, although structural data to support such changes remain elusive. Here, we describe the X-ray structure of dimeric BCL-W that reveals a major conformational change involving helices α3 and α4 hinging away from the core of the protein. Biochemical and functional studies reveal that the α4-α5 hinge region is required for dimerization of BCL-W, and functioning of both pro- and antiapoptotic BCL-2 proteins. Hence, this structure reveals a conformational flexibility not seen in previous BCL-2 protein structures and provides insights into how these regulators of apoptosis can change conformation to exert their function.

PubMed: 22000515
DOI: 10.1016/J.STR.2011.07.015

実験手法

X-RAY DIFFRACTION (2 Å)