2p1l

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[[Image:2p1l.gif|left|200px]]
[[Image:2p1l.gif|left|200px]]
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{{Structure
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|PDB= 2p1l |SIZE=350|CAPTION= <scene name='initialview01'>2p1l</scene>, resolution 2.50&Aring;
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The line below this paragraph, containing "STRUCTURE_2p1l", creates the "Structure Box" on the page.
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|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])
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{{STRUCTURE_2p1l| PDB=2p1l | SCENE= }}
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|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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'''Structure of the Bcl-XL:Beclin 1 complex'''
'''Structure of the Bcl-XL:Beclin 1 complex'''
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[[Category: Oberstein, A L.]]
[[Category: Oberstein, A L.]]
[[Category: Shi, Y.]]
[[Category: Shi, Y.]]
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[[Category: apoptosis]]
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[[Category: Apoptosis]]
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[[Category: autophagy]]
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[[Category: Autophagy]]
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[[Category: bcl]]
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[[Category: Bcl]]
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[[Category: beclin]]
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[[Category: Beclin]]
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[[Category: bh3 domain]]
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[[Category: Bh3 domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:08:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:27:04 2008''
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Revision as of 09:08, 4 May 2008

Image:2p1l.gif

Template:STRUCTURE 2p1l

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 Sun May 4 12:08:53 2008

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