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5W63

Crystal structure of channel catfish BAX

5W63 の概要
エントリーDOI10.2210/pdb5w63/pdb
関連するPDBエントリー5W5X 5W5Z 5W60 5W61 5W62
分子名称Apoptosis regulator bax, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
機能のキーワードbax, monomer, catfish, apoptosis
由来する生物種Ictalurus punctatus (Channel catfish)
タンパク質・核酸の鎖数1
化学式量合計21911.86
構造登録者
Robin, A.Y.,Colman, P.M.,Czabotar, P.E.,Luo, C.S. (登録日: 2017-06-16, 公開日: 2018-06-27, 最終更新日: 2023-10-04)
主引用文献Robin, A.Y.,Iyer, S.,Birkinshaw, R.W.,Sandow, J.,Wardak, A.,Luo, C.S.,Shi, M.,Webb, A.I.,Czabotar, P.E.,Kluck, R.M.,Colman, P.M.
Ensemble Properties of Bax Determine Its Function.
Structure, 26:1346-, 2018
Cited by
PubMed Abstract: BAX and BAK are essential mediators of intrinsic apoptosis that permeabilize the mitochondrial outer membrane. BAX activation requires its translocation from cytosol to mitochondria where conformational changes cause its oligomerization. To better understand the critical step of translocation, we examined its blockade by mutation near the C terminus (P168G) or by antibody binding near the N terminus. Similarities in the crystal structures of wild-type and BAX P168G but significant other differences suggest that cytosolic BAX exists as an ensemble of conformers, and that the distribution of conformers within the ensemble determines the different functions of wild-type and mutant proteins. We also describe the structure of BAX in complex with an antibody, 3C10, that inhibits cytosolic BAX by limiting exposure of the membrane-associating helix α9, as does the P168G mutation. Our data for both means of BAX inhibition argue for an allosteric model of BAX regulation that derives from properties of the ensemble of conformers.
PubMed: 30122452
DOI: 10.1016/j.str.2018.07.006
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.436 Å)
構造検証レポート
Validation report summary of 5w63
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2025-12-31に公開中

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