1PQ0

Crystal structure of mouse Bcl-xl

1PQ0 の概要

• エントリーDOI: 10.2210/pdb1pq0/pdb
• 関連するPDBエントリー: 1PQ1
• 分子名称: Apoptosis regulator Bcl-X (2 entities in total)
• 機能のキーワード: bcl-xl, apoptosis
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Isoform Bcl-X(L): Mitochondrion membrane. Isoform Bcl-X(delta-TM): Cytoplasm: Q64373
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22056.21

構造登録者

Liu, X.,Dai, S.,Zhu, Y.,Marrack, P.,Kappler, J.W. (登録日: 2003-06-17, 公開日: 2003-09-23, 最終更新日: 2023-08-16)

主引用文献

Liu, X.,Dai, S.,Zhu, Y.,Marrack, P.,Kappler, J.W.
The structure of a Bcl-xl/Bim fragment complex: Implications for Bim function
Immunity, 19:341-352, 2003

PubMed Abstract: After antigen-driven expansion, the majority of T cells involved in an immune response die rapidly by apoptosis dependent on the Bcl-2 related proteins, Bim and Bax or Bak. The details of how these proteins are activated and interact are still unclear. The crystal structure of mouse Bcl-x(L) bound to a long helical fragment of Bim indicates that the structure of Bim is very different from proteins with a Bcl-2-like fold and may leave the BH3 region of Bim constitutively exposed. Based on the structural homology between Bcl-x(L) and Bax, we predicted that binding of Bim to Bax would require displacement of the Bax penultimate alpha helix. Consistent with this prediction, truncation of this short helix was required for Bim/Bax interaction and led to spontaneous activation of Bax. Our results suggest a way in which both Bim and Bax/Bak might be required for activated T cell apoptosis.

PubMed: 14499110
DOI: 10.1016/S1074-7613(03)00234-6

実験手法

X-RAY DIFFRACTION (2.2 Å)