2pon
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(New page: 200px<br /> <applet load="2pon" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pon" /> '''Solution structure of the Bcl-xL/Beclin-1 c...)
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Revision as of 21:19, 12 November 2007
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Solution structure of the Bcl-xL/Beclin-1 complex
Overview
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.
About this Structure
2PON is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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., Feng W, Huang S, Wu H, Zhang M, J Mol Biol. 2007 Sep 7;372(1):223-35. Epub 2007 Jun 30. PMID:17659302
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