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1R2I

Human Bcl-XL containing a Phe to Leu mutation at position 146

1R2I の概要
エントリーDOI10.2210/pdb1r2i/pdb
関連するPDBエントリー1MAZ 1R2D 1R2E 1R2G 1R2H
分子名称Apoptosis regulator Bcl-X (2 entities in total)
機能のキーワードapoptosis, monomeric, alpha-helical, mutation
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24572.93
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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 1r2i
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-12-18に公開中

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