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首页> 外文期刊>Journal of Molecular Biology >Molecular basis of Bcl-xL's target recognition versatility revealed by the structure of Bcl-xL in complex with the BH3 domain of beclin-1
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Molecular basis of Bcl-xL's target recognition versatility revealed by the structure of Bcl-xL in complex with the BH3 domain of beclin-1

机译：Bcl-xL与beclin-1的BH3结构域复合的结构揭示了Bcl-xL靶标识别多功能性的分子基础

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摘要

Beclin-1, originally identified as a Bcl-2 binding protein, is an evolutionarily conserved protein required for autophagy. The direct interaction between Beclin-1 and Bcl-2 or Bcl-xL provides a potential convergence point for apoptosis and autophagy, two programmed cell death processes. Given the functional significance of the interaction between Beclin-1 and Bcl-2/Bcl-xL, we performed detailed biochemical and structural characterizations of this interaction. We demonstrated that the Bcl-xL-binding domain of Beclin-1 contains a BH3 domain. Therefore, Beclin-1 is a new member of the BH3 only family proteins. The structure of Bcl-xL in complex with the Beclin-1 BH3 domain was determined at high resolution by NMR spectroscopy. Although similar to other known BH3 domains, the Beclin-1 BH3 domain displays its own distinct features in the complex with Bcl-xL. Systematic analysis of all known Bcl-xL/BH3 domain complexes helped us to identify the molecular basis underlying the capacity of Bcl-xL to recognize diverse target sequences. (c) 2007 Elsevier Ltd. All rights reserved.
机译：最初被鉴定为Bcl-2结合蛋白的Beclin-1是自噬所需的进化保守蛋白。 Beclin-1和Bcl-2或Bcl-xL之间的直接相互作用为凋亡和自噬这两个程序性细胞死亡过程提供了潜在的收敛点。鉴于Beclin-1和Bcl-2 / Bcl-xL之间相互作用的功能重要性，我们对该相互作用进行了详细的生化和结构表征。我们证明了Beclin-1的Bcl-xL绑定域包含一个BH3域。因此，Beclin-1是仅BH3家族蛋白的新成员。与Beclin-1 BH3域复合的Bcl-xL的结构是通过NMR光谱法高分辨率确定的。尽管与其他已知的BH3域相似，但Beclin-1 BH3域在与Bcl-xL形成的复合物中显示出其独特的特征。对所有已知的Bcl-xL / BH3结构域复合物的系统分析帮助我们确定了Bcl-xL识别各种靶序列的能力基础的分子基础。 （c）2007 Elsevier Ltd.保留所有权利。

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