1R2D

Structure of Human Bcl-XL at 1.95 Angstroms

1R2D の概要

• エントリーDOI: 10.2210/pdb1r2d/pdb
• 関連するPDBエントリー: 1MAZ 1R2E 1R2G 1R2H 1R2I
• 分子名称: Apoptosis regulator Bcl-X (2 entities in total)
• 機能のキーワード: apoptosis, monomeric, alpha-helical
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Isoform Bcl-X(L): Mitochondrion inner membrane : Q07817
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24606.94

構造登録者

O'Neill, J.W.,Manion, M.K.,Giedt, C.D.,Kim, K.M.,Zhang, K.Y.,Hockenbery, D.M. (登録日: 2003-09-26, 公開日: 2004-02-03, 最終更新日: 2023-08-23)

主引用文献

Manion, M.K.,O'Neill, J.W.,Giedt, C.D.,Kim, K.M.,Zhang, K.Y.,Hockenbery, D.M.
Bcl-XL mutations suppress cellular sensitivity to antimycin A.
J.Biol.Chem., 279:2159-2165, 2004

PubMed Abstract: Cells expressing high levels of the BCL-X(L) anti-apoptotic protein are preferentially killed by the mitochondrial inhibitor antimycin A (AA). Computational modeling predicts a binding site for AA in the extended hydrophobic groove on BCL-X(L), previously identified as an interface for dimerization to BAX and related proapoptotic proteins. Here, we identify BCL-X(L) hydrophobic groove mutants with normal cellular anti-apoptotic function but suppressed sensitivity to AA. The LD(50) of AA for cells expressing BCL-X(L) mutants directly correlates with the measured in vitro dissociation constants for AA binding. These results indicate that BCL-X(L) is a principal target mediating AA cytotoxicity.

PubMed: 14534311
DOI: 10.1074/jbc.M306021200

実験手法

X-RAY DIFFRACTION (1.95 Å)