2PON
Solution structure of the Bcl-xL/Beclin-1 complex
Summary for 2PON
| Entry DOI | 10.2210/pdb2pon/pdb |
| Descriptor | Beclin-1, Apoptosis regulator Bcl-X (2 entities in total) |
| Functional Keywords | apoptosis; autophagy; bcl-2 family proteins; beclin-1, apoptosis inhibitor |
| Biological source | Homo sapiens (human) More |
| Cellular location | Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein: Q14457 Mitochondrion membrane; Single-pass membrane protein (By similarity): Q07817 |
| Total number of polymer chains | 2 |
| Total formula weight | 20398.60 |
| Authors | |
| Primary citation | Feng, W.,Huang, S.,Wu, H.,Zhang, M. 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. J.Mol.Biol., 372:223-235, 2007 Cited by PubMed Abstract: 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. PubMed: 17659302DOI: 10.1016/j.jmb.2007.06.069 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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