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2p1l

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[[Image:2p1l.gif|left|200px]]
 
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==Structure of the Bcl-XL:Beclin 1 complex==
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The line below this paragraph, containing "STRUCTURE_2p1l", creates the "Structure Box" on the page.
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<StructureSection load='2p1l' size='340' side='right'caption='[[2p1l]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2p1l]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P1L FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2p1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p1l OCA], [https://pdbe.org/2p1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p1l RCSB], [https://www.ebi.ac.uk/pdbsum/2p1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p1l ProSAT]</span></td></tr>
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{{STRUCTURE_2p1l| PDB=2p1l | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/B2CL1_HUMAN B2CL1_HUMAN] Potent inhibitor of cell death. Inhibits activation of caspases (By similarity). Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis.<ref>PMID:19917720</ref> <ref>PMID:21840391</ref> Isoform Bcl-X(S) promotes apoptosis.<ref>PMID:19917720</ref> <ref>PMID:21840391</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p1/2p1l_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2p1l ConSurf].
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<div style="clear:both"></div>
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'''Structure of the Bcl-XL:Beclin 1 complex'''
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==See Also==
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*[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]]
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== References ==
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==Overview==
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<references/>
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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.
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__TOC__
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</StructureSection>
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==About this Structure==
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2P1L is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P1L OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17337444 17337444]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Jeffrey, P D.]]
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[[Category: Jeffrey PD]]
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[[Category: Oberstein, A L.]]
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[[Category: Oberstein AL]]
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[[Category: Shi, Y.]]
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[[Category: Shi Y]]
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[[Category: Apoptosis]]
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[[Category: Autophagy]]
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[[Category: Bcl]]
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[[Category: Beclin]]
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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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Current revision

Structure of the Bcl-XL:Beclin 1 complex

PDB ID 2p1l

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