2yv6: Difference between revisions

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[[Image:2yv6.png|left|200px]]


{{STRUCTURE_2yv6| PDB=2yv6 | SCENE= }}
==Crystal structure of human Bcl-2 family protein Bak==
<StructureSection load='2yv6' size='340' side='right'caption='[[2yv6]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2yv6]] is a 1 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=2YV6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YV6 FirstGlance]. <br>
</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>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2yv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yv6 OCA], [https://pdbe.org/2yv6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yv6 RCSB], [https://www.ebi.ac.uk/pdbsum/2yv6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yv6 ProSAT], [https://www.topsan.org/Proteins/RSGI/2yv6 TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BAK_HUMAN BAK_HUMAN] In the presence of an appropriate stimulus, accelerates programmed cell death by binding to, and antagonizing the anti-apoptotic action of BCL2 or its adenovirus homolog E1B 19k protein. Low micromolar levels of zinc ions inhibit the promotion of apoptosis.<ref>PMID:8521816</ref> <ref>PMID:17157251</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/yv/2yv6_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2yv6 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Interactions of Bcl-2 family proteins play a regulatory role in mitochondrial apoptosis. The pro-apoptotic protein Bak resides in the outer mitochondrial membrane, and the formation of Bak homo- or heterodimers is involved in the regulation of apoptosis. The previously reported structure of the human Bak protein (residues Glu16-Gly186) revealed that a zinc ion was coordinated with two pairs of Asp160 and His164 residues from the symmetry-related molecules. This zinc-dependent homodimer was regarded as an anti-apoptotic dimer. In the present study, we determined the crystal structure of the human Bak residues Ser23-Asn185 at 2.5A, and found a distinct type of homodimerization through Cys166 disulfide bridging between the symmetry-related molecules. In the two modes of homodimerization, the molecular interfaces are completely different. In the membrane-targeted model of the S-S bridged dimer, the BH3 motifs are too close to the membrane to interact directly with the anti-apoptotic relatives, such as Bcl-x(L). Therefore, the Bak dimer structure reported here may represent a pro-apoptotic mode under oxidized conditions.


===Crystal structure of human Bcl-2 family protein Bak===
Novel dimerization mode of the human Bcl-2 family protein Bak, a mitochondrial apoptosis regulator.,Wang H, Takemoto C, Akasaka R, Uchikubo-Kamo T, Kishishita S, Murayama K, Terada T, Chen L, Liu ZJ, Wang BC, Sugano S, Tanaka A, Inoue M, Kigawa T, Shirouzu M, Yokoyama S J Struct Biol. 2009 Apr;166(1):32-7. Epub 2008 Dec 24. PMID:19135534<ref>PMID:19135534</ref>


{{ABSTRACT_PUBMED_19135534}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 2yv6" style="background-color:#fffaf0;"></div>
[[2yv6]] is a 1 chain structure with sequence 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=2YV6 OCA].


==See Also==
==See Also==
*[[Bcl-2|Bcl-2]]
*[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:019135534</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Kishishita, S.]]
[[Category: Large Structures]]
[[Category: Murayama, K.]]
[[Category: Kishishita S]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Murayama K]]
[[Category: Shirouzu, M.]]
[[Category: Shirouzu M]]
[[Category: Takemoto, C.]]
[[Category: Takemoto C]]
[[Category: Terada, T.]]
[[Category: Terada T]]
[[Category: Wang, H.]]
[[Category: Wang H]]
[[Category: Apoptosis]]
[[Category: Bcl domain]]
[[Category: National project on protein structural and functional analyse]]
[[Category: Nppsfa]]
[[Category: Riken structural genomics/proteomics initiative]]
[[Category: Rsgi]]
[[Category: Structure genomic]]
Retrieved from "https://proteopedia.org/2yv6"