2pon

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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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==Reference==
==Reference==
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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., Feng W, Huang S, Wu H, Zhang M, J Mol Biol. 2007 Sep 7;372(1):223-35. Epub 2007 Jun 30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17659302 17659302]
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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., Feng W, Huang S, Wu H, Zhang M, J Mol Biol. 2007 Sep 7;372(1):223-35. Epub 2007 Jun 30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17659302 17659302]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: apoptosis; autophagy; bcl-2 family proteins; beclin-1]]
[[Category: apoptosis; autophagy; bcl-2 family proteins; beclin-1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:46:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:31:37 2008''

Revision as of 16:31, 21 February 2008


2pon

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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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