2P1L
Structure of the Bcl-XL:Beclin 1 complex
2P1L の概要
| エントリーDOI | 10.2210/pdb2p1l/pdb |
| 分子名称 | Apoptosis regulator Bcl-X, Beclin 1 (3 entities in total) |
| 機能のキーワード | apoptosis; autophagy; beclin; bh3 domain; bcl, apoptosis |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| 細胞内の位置 | Isoform Bcl-X(L): Mitochondrion inner membrane : Q07817 Cytoplasm . Beclin-1-C 35 kDa: Mitochondrion . Beclin-1-C 37 kDa: Mitochondrion : Q14457 |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 83553.02 |
| 構造登録者 | |
| 主引用文献 | Oberstein, A.,Jeffrey, P.D.,Shi, Y. Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein J.Biol.Chem., 282:13123-13132, 2007 Cited by PubMed Abstract: Bcl-2 family proteins are key regulators of apoptosis and have recently been shown to modulate autophagy. The tumor suppressor Beclin 1 has been proposed to coordinate both apoptosis and autophagy through direct interaction with anti-apoptotic family members Bcl-2 and/or Bcl-X(L). However, the molecular basis for this interaction remains enigmatic. Here we report that Beclin 1 contains a conserved BH3 domain, which is both necessary and sufficient for its interaction with Bcl-X(L). We also report the crystal structure of a Beclin BH3 peptide in complex with Bcl-X(L) at 2.5A resolution. Reminiscent of previously determined Bcl-X(L)-BH3 structures, the amphipathic BH3 helix of Beclin 1 bound to a conserved hydrophobic groove of Bcl-X(L). These results define Beclin 1 as a novel BH3-only protein, implying that Beclin 1 may have a direct role in initiating apoptotic signaling. We propose that this putative apoptotic function may be linked to the ability of Beclin 1 to suppress tumor formation in mammals. PubMed: 17337444DOI: 10.1074/jbc.M700492200 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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