1DDB
STRUCTURE OF MOUSE BID, NMR, 20 STRUCTURES
1DDB の概要
| エントリーDOI | 10.2210/pdb1ddb/pdb |
| 分子名称 | PROTEIN (BID) (1 entity in total) |
| 機能のキーワード | apoptosis, programmed cell death, bcl-2 family, bh3 domain |
| 由来する生物種 | Mus musculus (house mouse) |
| 細胞内の位置 | Cytoplasm: P70444 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 21974.63 |
| 構造登録者 | Mcdonnell, J.M.,Fushman, D.,Milliman, C.,Korsmeyer, S.J.,Cowburn, D. (登録日: 1999-02-19, 公開日: 1999-08-30, 最終更新日: 2023-12-27) |
| 主引用文献 | McDonnell, J.M.,Fushman, D.,Milliman, C.L.,Korsmeyer, S.J.,Cowburn, D. Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists. Cell(Cambridge,Mass.), 96:625-634, 1999 Cited by PubMed Abstract: Members of the BCL2 family of proteins are key regulators of programmed cell death, acting either as apoptotic agonists or antagonists. Here we describe the solution structure of BID, presenting the structure of a proapoptotic BCL2 family member. An analysis of sequence/structure of BCL2 family members allows us to define a structural superfamily, which has implications for general mechanisms for regulating proapoptotic activity. It appears two criteria must be met for proapoptotic function within the BCL2 family: targeting of molecules to intracellular membranes, and exposure of the BH3 death domain. BID's activity is regulated by a Caspase 8-mediated cleavage event, exposing the BH3 domain and significantly changing the surface charge and hydrophobicity, resulting in a change of cellular localization. PubMed: 10089878DOI: 10.1016/S0092-8674(00)80573-5 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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