2imt
From Proteopedia
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| - | [[Image:2imt.png|left|200px]]  | ||
| - | + | ==The X-ray Structure of a Bak Homodimer Reveals an Inhibitory Zinc Binding Site==  | |
| + | <StructureSection load='2imt' size='340' side='right'caption='[[2imt]], [[Resolution|resolution]] 1.49Å' scene=''>  | ||
| + | == Structural highlights ==  | ||
| + | <table><tr><td colspan='2'>[[2imt]] 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=2IMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IMT 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]] 1.49Å</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>  | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2imt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2imt OCA], [https://pdbe.org/2imt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2imt RCSB], [https://www.ebi.ac.uk/pdbsum/2imt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2imt ProSAT]</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/im/2imt_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=2imt ConSurf].  | ||
| + | <div style="clear:both"></div>  | ||
| + | <div style="background-color:#fffaf0;">  | ||
| + | == Publication Abstract from PubMed ==  | ||
| + | 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.  | ||
| - | + | 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>  | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>  | |
| - | + | </div>  | |
| - | + | <div class="pdbe-citations 2imt" style="background-color:#fffaf0;"></div>  | |
| - | + | == References ==  | |
| - | + | <references/>  | |
| - | ==  | + | __TOC__  | 
| - | + | </StructureSection>  | |
| - | + | ||
| - | ==  | + | |
| - | <  | + | |
[[Category: Homo sapiens]]  | [[Category: Homo sapiens]]  | ||
| - | [[Category: Gehring  | + | [[Category: Large Structures]]  | 
| - | [[Category: Liu  | + | [[Category: Gehring KB]]  | 
| - | [[Category: Moldoveanu  | + | [[Category: Liu Q]]  | 
| - | [[Category: Shore  | + | [[Category: Moldoveanu T]]  | 
| - | [[Category: Tocilj  | + | [[Category: Shore GC]]  | 
| - | [[Category: Watson  | + | [[Category: Tocilj A]]  | 
| - | + | [[Category: Watson M]]  | |
| - | + | ||
Current revision
The X-ray Structure of a Bak Homodimer Reveals an Inhibitory Zinc Binding Site
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Categories: Homo sapiens | Large Structures | Gehring KB | Liu Q | Moldoveanu T | Shore GC | Tocilj A | Watson M

