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1zy3

From Proteopedia

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[[Image:1zy3.gif|left|200px]]
 
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==Structural model of complex of Bcl-w protein with Bid BH3-peptide==
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The line below this paragraph, containing "STRUCTURE_1zy3", creates the "Structure Box" on the page.
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<StructureSection load='1zy3' size='340' side='right'caption='[[1zy3]]' 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'>[[1zy3]] is a 2 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=1ZY3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZY3 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">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=1zy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zy3 OCA], [https://pdbe.org/1zy3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zy3 RCSB], [https://www.ebi.ac.uk/pdbsum/1zy3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zy3 ProSAT]</span></td></tr>
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{{STRUCTURE_1zy3| PDB=1zy3 | SCENE= }}
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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/zy/1zy3_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=1zy3 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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A peptide corresponding to the BH3 region of the proapoptotic protein, BID, could be bound in the cleft of the antiapoptotic protein, BCL-w. This binding induced major conformational rearrangements in both the peptide and protein components of the complex and led to the displacement and unfolding of the BCL-w C-terminal alpha-helix. The structure of BCL-w with a bound BID-BH3 peptide was determined using NMR spectroscopy and molecular docking. These studies confirmed that a region of 16 residues of the BID-BH3 peptide is responsible for its strong binding to BCL-w and BCL-x(L). The interactions of BCL-w and the BID-BH3 peptide complex with dodecylphosphocholine micelles were characterized and showed that the conformational change of BCL-w upon lipid binding occurred at the same time as the release and unfolding of the BH3 peptide.
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'''Structural model of complex of Bcl-w protein with Bid BH3-peptide'''
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Structural model of the BCL-w-BID peptide complex and its interactions with phospholipid micelles.,Denisov AY, Chen G, Sprules T, Moldoveanu T, Beauparlant P, Gehring K Biochemistry. 2006 Feb 21;45(7):2250-6. PMID:16475813<ref>PMID:16475813</ref>
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==Overview==
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A peptide corresponding to the BH3 region of the proapoptotic protein, BID, could be bound in the cleft of the antiapoptotic protein, BCL-w. This binding induced major conformational rearrangements in both the peptide and protein components of the complex and led to the displacement and unfolding of the BCL-w C-terminal alpha-helix. The structure of BCL-w with a bound BID-BH3 peptide was determined using NMR spectroscopy and molecular docking. These studies confirmed that a region of 16 residues of the BID-BH3 peptide is responsible for its strong binding to BCL-w and BCL-x(L). The interactions of BCL-w and the BID-BH3 peptide complex with dodecylphosphocholine micelles were characterized and showed that the conformational change of BCL-w upon lipid binding occurred at the same time as the release and unfolding of the BH3 peptide.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1ZY3 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=1ZY3 OCA].
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</div>
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<div class="pdbe-citations 1zy3" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Structural model of the BCL-w-BID peptide complex and its interactions with phospholipid micelles., Denisov AY, Chen G, Sprules T, Moldoveanu T, Beauparlant P, Gehring K, Biochemistry. 2006 Feb 21;45(7):2250-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16475813 16475813]
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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>
[[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: Denisov, A Y.]]
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[[Category: Denisov AY]]
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[[Category: Gehring, K.]]
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[[Category: Gehring K]]
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[[Category: Apoptosis]]
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[[Category: Bcl-w]]
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[[Category: Bh3-peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:13:26 2008''
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Current revision

Structural model of complex of Bcl-w protein with Bid BH3-peptide

PDB ID 1zy3

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