4BD8

Bax domain swapped dimer induced by BimBH3 with CHAPS

4BD8 の概要

• エントリーDOI: 10.2210/pdb4bd8/pdb
• 関連するPDBエントリー: 4BD2 4BD6 4BD7 4BDU
• 分子名称: APOPTOSIS REGULATOR BAX, PRASEODYMIUM ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: apoptosis, programmed cell death
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Isoform Alpha: Mitochondrion membrane; Single-pass membrane protein. Isoform Beta: Cytoplasm. Isoform Gamma: Cytoplasm. Isoform Delta: Cytoplasm (Potential): Q07812
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 77509.20

構造登録者

Czabotar, P.E.,Westphal, D.,Adams, J.M.,Colman, P.M. (登録日: 2012-10-05, 公開日: 2013-02-13, 最終更新日: 2024-05-01)

主引用文献

Czabotar, P.E.,Westphal, D.,Dewson, G.,Ma, S.,Hockings, C.,Fairlie, W.D.,Lee, E.F.,Yao, S.,Robin, A.Y.,Smith, B.J.,Huang, D.C.,Kluck, R.M.,Adams, J.M.,Colman, P.M.
Bax Crystal Structures Reveal How Bh3 Domains Activate Bax and Nucleate its Oligomerization to Induce Apoptosis.
Cell(Cambridge,Mass.), 152:519-, 2013

PubMed Abstract: In stressed cells, apoptosis ensues when Bcl-2 family members Bax or Bak oligomerize and permeabilize the mitochondrial outer membrane. Certain BH3-only relatives can directly activate them to mediate this pivotal, poorly understood step. To clarify the conformational changes that induce Bax oligomerization, we determined crystal structures of BaxΔC21 treated with detergents and BH3 peptides. The peptides bound the Bax canonical surface groove but, unlike their complexes with prosurvival relatives, dissociated Bax into two domains. The structures define the sequence signature of activator BH3 domains and reveal how they can activate Bax via its groove by favoring release of its BH3 domain. Furthermore, Bax helices α2-α5 alone adopted a symmetric homodimer structure, supporting the proposal that two Bax molecules insert their BH3 domain into each other's surface groove to nucleate oligomerization. A planar lipophilic surface on this homodimer may engage the membrane. Our results thus define critical Bax transitions toward apoptosis.

PubMed: 23374347
DOI: 10.1016/J.CELL.2012.12.031

実験手法

X-RAY DIFFRACTION (2.22 Å)