8SRY

Crystal structure of BAK-BAX heterodimer with C12E8

8SRY の概要

• エントリーDOI: 10.2210/pdb8sry/pdb
• 分子名称: Bcl-2 homologous antagonist/killer, Apoptosis regulator BAX, 2-(2-METHOXYETHOXY)ETHANOL, ... (8 entities in total)
• 機能のキーワード: bax, bak, bcl2, apoptosis
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 38507.34

構造登録者

Brouwer, J.M.,Czabotar, P.E.,Colman, P.M.,Miller, M.S. (登録日: 2023-05-08, 公開日: 2023-12-27, 最終更新日: 2024-06-19)

主引用文献

Miller, M.S.,Cowan, A.D.,Brouwer, J.M.,Smyth, S.T.,Peng, L.,Wardak, A.Z.,Uren, R.T.,Luo, C.,Roy, M.J.,Shah, S.,Tan, Z.,Reid, G.E.,Colman, P.M.,Czabotar, P.E.
Sequence differences between BAX and BAK core domains manifest as differences in their interactions with lipids.
Febs J., 291:2335-2353, 2024

PubMed Abstract: The B-cell lymphoma 2 (BCL2) family members, BCL2-associated protein X (BAX) and BCL2 homologous antagonist killer (BAK), are required for programmed cell death via the mitochondrial pathway. When cells are stressed, damaged or redundant, the balance of power between the BCL2 family of proteins shifts towards BAX and BAK, allowing their transition from an inactive, monomeric state to a membrane-active oligomeric form that releases cytochrome c from the mitochondrial intermembrane space. That oligomeric state has an essential intermediate, a symmetric homodimer of BAX or BAK. Here we describe crystal structures of dimers of the core domain of BAX, comprising its helices α2-α5. These structures provide an atomic resolution description of the interactions that drive BAX homo-dimerisation and insights into potential interaction between core domain dimers and membrane lipids. The previously identified BAK lipid-interacting sites are not conserved with BAX and are likely to determine the differences between them in their interactions with lipids. We also describe structures of heterodimers of BAK/BAX core domains, yielding further insight into the differences in lipid binding between BAX and BAK.

PubMed: 38088212
DOI: 10.1111/febs.17031

実験手法

X-RAY DIFFRACTION (2.4 Å)