1zy3: Difference between revisions

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[[Image:1zy3.gif|left|200px]]


{{Structure
==Structural model of complex of Bcl-w protein with Bid BH3-peptide==
|PDB= 1zy3 |SIZE=350|CAPTION= <scene name='initialview01'>1zy3</scene>
<StructureSection load='1zy3' size='340' side='right'caption='[[1zy3]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<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>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
|GENE=  
<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>
}}
</table>
== Function ==
[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>  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zy/1zy3_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


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


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1zy3" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]]
 
== References ==
==About this Structure==
<references/>
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].
__TOC__
 
</StructureSection>
==Reference==
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]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Denisov, A Y.]]
[[Category: Denisov AY]]
[[Category: Gehring, K.]]
[[Category: Gehring K]]
[[Category: apoptosis]]
[[Category: bcl-w]]
[[Category: bh3-peptide]]
 
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Retrieved from "https://proteopedia.org/1zy3"