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2ims

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[[Image:2ims.jpg|left|200px]]
 
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==The X-ray Structure of a Bak Homodimer Reveals an Inhibitory Zinc Binding Site==
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The line below this paragraph, containing "STRUCTURE_2ims", creates the "Structure Box" on the page.
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<StructureSection load='2ims' size='340' side='right'caption='[[2ims]], [[Resolution|resolution]] 1.48&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'>[[2ims]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IMS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IMS FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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-->
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_2ims| PDB=2ims | SCENE= }}
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1maz|1maz]], [[1f16|1f16]], [[1lxl|1lxl]], [[1bxl|1bxl]], [[1mk3|1mk3]], [[1wsx|1wsx]], [[2imt|2imt]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAK1, BAK, BCL2L7 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2ims FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ims OCA], [https://pdbe.org/2ims PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ims RCSB], [https://www.ebi.ac.uk/pdbsum/2ims PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ims ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[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>
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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/im/2ims_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=2ims 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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BAK/BAX-mediated mitochondrial outer-membrane permeabilization (MOMP) drives cell death during development and tissue homeostasis from zebrafish to humans. In most cancers, this pathway is inhibited by BCL-2 family antiapoptotic members, which bind and block the action of proapoptotic BCL proteins. We report the 1.5 A crystal structure of calpain-proteolysed BAK, cBAK, to reveal a zinc binding site that regulates its activity via homodimerization. cBAK contains an occluded BH3 peptide binding pocket that binds a BID BH3 peptide only weakly . Nonetheless, cBAK requires activation by truncated BID to induce cytochrome c release in mitochondria isolated from bak/bax double-knockout mouse embryonic fibroblasts. The BAK-mediated MOMP is inhibited by low micromolar zinc levels. This inhibition is alleviated by mutation of the zinc-coordination site in BAK. Our results link directly the antiapoptotic effects of zinc to BAK.
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'''The X-ray Structure of a Bak Homodimer Reveals an Inhibitory Zinc Binding Site'''
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The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site.,Moldoveanu T, Liu Q, Tocilj A, Watson M, Shore G, Gehring K Mol Cell. 2006 Dec 8;24(5):677-88. PMID:17157251<ref>PMID:17157251</ref>
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==Overview==
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BAK/BAX-mediated mitochondrial outer-membrane permeabilization (MOMP) drives cell death during development and tissue homeostasis from zebrafish to humans. In most cancers, this pathway is inhibited by BCL-2 family antiapoptotic members, which bind and block the action of proapoptotic BCL proteins. We report the 1.5 A crystal structure of calpain-proteolysed BAK, cBAK, to reveal a zinc binding site that regulates its activity via homodimerization. cBAK contains an occluded BH3 peptide binding pocket that binds a BID BH3 peptide only weakly . Nonetheless, cBAK requires activation by truncated BID to induce cytochrome c release in mitochondria isolated from bak/bax double-knockout mouse embryonic fibroblasts. The BAK-mediated MOMP is inhibited by low micromolar zinc levels. This inhibition is alleviated by mutation of the zinc-coordination site in BAK. Our results link directly the antiapoptotic effects of zinc to BAK.
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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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2IMS is a [[Single protein]] structure of 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=2IMS OCA].
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</div>
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<div class="pdbe-citations 2ims" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site., Moldoveanu T, Liu Q, Tocilj A, Watson M, Shore G, Gehring K, Mol Cell. 2006 Dec 8;24(5):677-88. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17157251 17157251]
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*[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]]
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[[Category: Homo sapiens]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Gehring, K B.]]
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__TOC__
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[[Category: Liu, Q.]]
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</StructureSection>
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[[Category: Moldoveanu, T.]]
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[[Category: Human]]
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[[Category: Shore, G C.]]
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[[Category: Large Structures]]
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[[Category: Tocilj, A.]]
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[[Category: Gehring, K B]]
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[[Category: Watson, M.]]
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[[Category: Liu, Q]]
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[[Category: Moldoveanu, T]]
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[[Category: Shore, G C]]
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[[Category: Tocilj, A]]
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[[Category: Watson, M]]
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[[Category: Apoptosis]]
[[Category: Dimer]]
[[Category: Dimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:40:14 2008''
 

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The X-ray Structure of a Bak Homodimer Reveals an Inhibitory Zinc Binding Site

PDB ID 2ims

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