2p1l
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= BCL2L1, BCL2L, BCLX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), BECN1, GT197 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= BCL2L1, BCL2L, BCLX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), BECN1, GT197 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p1l OCA], [http://www.ebi.ac.uk/pdbsum/2p1l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2p1l RCSB]</span> | ||
}} | }} | ||
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[[Category: Oberstein, A L.]] | [[Category: Oberstein, A L.]] | ||
[[Category: Shi, Y.]] | [[Category: Shi, Y.]] | ||
| - | [[Category: apoptosis | + | [[Category: apoptosis]] |
| + | [[Category: autophagy]] | ||
| + | [[Category: bcl]] | ||
| + | [[Category: beclin]] | ||
| + | [[Category: bh3 domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:27:04 2008'' |
Revision as of 01:27, 31 March 2008
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | BCL2L1, BCL2L, BCLX (Homo sapiens), BECN1, GT197 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the Bcl-XL:Beclin 1 complex
Overview
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.
About this Structure
2P1L is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein., Oberstein A, Jeffrey PD, Shi Y, J Biol Chem. 2007 Apr 27;282(17):13123-32. Epub 2007 Mar 2. PMID:17337444
Page seeded by OCA on Mon Mar 31 04:27:04 2008
Categories: Homo sapiens | Protein complex | Jeffrey, P D. | Oberstein, A L. | Shi, Y. | Apoptosis | Autophagy | Bcl | Beclin | Bh3 domain
