4U2U

Bak domain swapped dimer induced by BidBH3 with CHAPS

4U2U の概要

• エントリーDOI: 10.2210/pdb4u2u/pdb
• 関連するPDBエントリー: 4U2V
• 分子名称: Bcl-2 homologous antagonist/killer (2 entities in total)
• 機能のキーワード: apoptosis, bak, bcl-2
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37960.54

構造登録者

Brouwer, J.M.,Colman, P.M.,Czabotar, P.E. (登録日: 2014-07-18, 公開日: 2014-09-10, 最終更新日: 2023-09-27)

主引用文献

Brouwer, J.M.,Westphal, D.,Dewson, G.,Robin, A.Y.,Uren, R.T.,Bartolo, R.,Thompson, G.V.,Colman, P.M.,Kluck, R.M.,Czabotar, P.E.
Bak Core and Latch Domains Separate during Activation, and Freed Core Domains Form Symmetric Homodimers.
Mol.Cell, 55:938-946, 2014

PubMed Abstract: Apoptotic stimuli activate and oligomerize the proapoptotic proteins Bak and Bax, resulting in mitochondrial outer-membrane permeabilization and subsequent cell death. This activation can occur when certain BH3-only proteins interact directly with Bak and Bax. Recently published crystal structures reveal that Bax separates into core and latch domains in response to BH3 peptides. The distinguishing characteristics of BH3 peptides capable of directly activating Bax were also elucidated. Here we identify specific BH3 peptides capable of "unlatching" Bak and describe structural insights into Bak activation and oligomerization. Crystal structures and crosslinking experiments demonstrate that Bak undergoes a conformational change similar to that of Bax upon activation. A structure of the Bak core domain dimer provides a high-resolution image of this key intermediate in the pore-forming oligomer. Our results confirm an analogous mechanism for activation and dimerization of Bak and Bax in response to certain BH3 peptides.

PubMed: 25175025
DOI: 10.1016/j.molcel.2014.07.016

実験手法

X-RAY DIFFRACTION (2.9 Å)