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1o0l

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(New page: 200px<br /> <applet load="1o0l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o0l" /> '''THE STRUCTURE OF BCL-W REVEALS A ROLE FOR T...)
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[[Image:1o0l.gif|left|200px]]<br />
 
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<applet load="1o0l" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1o0l" />
 
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'''THE STRUCTURE OF BCL-W REVEALS A ROLE FOR THE C-TERMINAL RESIDUES IN MODULATING BIOLOGICAL ACTIVITY'''<br />
 
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==Overview==
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==THE STRUCTURE OF BCL-W REVEALS A ROLE FOR THE C-TERMINAL RESIDUES IN MODULATING BIOLOGICAL ACTIVITY==
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Pro-survival Bcl-2-related proteins, critical regulators of apoptosis, contain a hydrophobic groove targeted for binding by the BH3 domain of the, pro-apoptotic BH3-only proteins. The solution structure of the, pro-survival protein Bcl-w, presented here, reveals that the binding, groove is not freely accessible as predicted by previous structures of, pro-survival Bcl-2-like molecules. Unexpectedly, the groove appears to be, occluded by the C-terminal residues. Binding and kinetic data suggest that, the C-terminal residues of Bcl-w and Bcl-x(L) modulate pro-survival, activity by regulating ligand access to the groove. Binding of the, BH3-only proteins, critical for cell death initiation, is likely to, displace the hydrophobic C-terminal region of Bcl-w and Bcl-x(L)., Moreover, Bcl-w does not act only by sequestering the BH3-only proteins., There fore, pro-survival Bcl-2-like molecules probably control the, activation of downstream effectors by a mechanism that remains to be, elucidated.
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<StructureSection load='1o0l' size='340' side='right'caption='[[1o0l]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1o0l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O0L FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1o0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o0l OCA], [https://pdbe.org/1o0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o0l RCSB], [https://www.ebi.ac.uk/pdbsum/1o0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o0l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/B2CL2_HUMAN B2CL2_HUMAN] Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX.<ref>PMID:8761287</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/o0/1o0l_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=1o0l ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Pro-survival Bcl-2-related proteins, critical regulators of apoptosis, contain a hydrophobic groove targeted for binding by the BH3 domain of the pro-apoptotic BH3-only proteins. The solution structure of the pro-survival protein Bcl-w, presented here, reveals that the binding groove is not freely accessible as predicted by previous structures of pro-survival Bcl-2-like molecules. Unexpectedly, the groove appears to be occluded by the C-terminal residues. Binding and kinetic data suggest that the C-terminal residues of Bcl-w and Bcl-x(L) modulate pro-survival activity by regulating ligand access to the groove. Binding of the BH3-only proteins, critical for cell death initiation, is likely to displace the hydrophobic C-terminal region of Bcl-w and Bcl-x(L). Moreover, Bcl-w does not act only by sequestering the BH3-only proteins. There fore, pro-survival Bcl-2-like molecules probably control the activation of downstream effectors by a mechanism that remains to be elucidated.
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==About this Structure==
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The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity.,Hinds MG, Lackmann M, Skea GL, Harrison PJ, Huang DC, Day CL EMBO J. 2003 Apr 1;22(7):1497-507. PMID:12660157<ref>PMID:12660157</ref>
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1O0L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O0L OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity., Hinds MG, Lackmann M, Skea GL, Harrison PJ, Huang DC, Day CL, EMBO J. 2003 Apr 1;22(7):1497-507. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12660157 12660157]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 1o0l" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Day, C.L.]]
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[[Category: Harrison, P.J.]]
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[[Category: Hinds, M.G.]]
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[[Category: Huang, D.C.S.]]
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[[Category: Lackmann, M.]]
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[[Category: Skea, G.L.]]
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[[Category: apoptosis]]
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[[Category: bcl-2]]
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[[Category: bh3]]
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[[Category: binding groove]]
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[[Category: helical bundle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:27:56 2007''
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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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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Day CL]]
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[[Category: Harrison PJ]]
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[[Category: Hinds MG]]
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[[Category: Huang DCS]]
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[[Category: Lackmann M]]
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[[Category: Skea GL]]

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THE STRUCTURE OF BCL-W REVEALS A ROLE FOR THE C-TERMINAL RESIDUES IN MODULATING BIOLOGICAL ACTIVITY

PDB ID 1o0l

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