6eb6
From Proteopedia
(Difference between revisions)
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<StructureSection load='6eb6' size='340' side='right'caption='[[6eb6]], [[Resolution|resolution]] 2.02Å' scene=''> | <StructureSection load='6eb6' size='340' side='right'caption='[[6eb6]], [[Resolution|resolution]] 2.02Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6eb6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EB6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EB6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6eb6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EB6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EB6 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAX, BCL2L4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6eb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eb6 OCA], [http://pdbe.org/6eb6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eb6 RCSB], [http://www.ebi.ac.uk/pdbsum/6eb6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eb6 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6eb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eb6 OCA], [http://pdbe.org/6eb6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eb6 RCSB], [http://www.ebi.ac.uk/pdbsum/6eb6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eb6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/BAX_HUMAN BAX_HUMAN]] Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis.<ref>PMID:8358790</ref> <ref>PMID:10772918</ref> <ref>PMID:8521816</ref> <ref>PMID:16113678</ref> <ref>PMID:18948948</ref> <ref>PMID:21199865</ref> | [[http://www.uniprot.org/uniprot/BAX_HUMAN BAX_HUMAN]] Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis.<ref>PMID:8358790</ref> <ref>PMID:10772918</ref> <ref>PMID:8521816</ref> <ref>PMID:16113678</ref> <ref>PMID:18948948</ref> <ref>PMID:21199865</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | To elicit apoptosis, BAX metamorphoses from an inert cytosolic monomer into homo-oligomers that permeabilize the mitochondrial outer membrane (MOM). A long-standing puzzle is that BH3 domains apparently activate BAX by not only its canonical groove but also a proposed site involving helices alpha1 and alpha6. Our mutagenesis studies reveal that late steps like oligomerization require activation through the groove but probably not earlier steps like MOM association. Conversely, alpha1 or alpha6 obstruction and alanine mutagenesis scanning implicate these helices early in BAX activation. The alpha1 and alpha6 mutations lowered BH3 binding, altered the BAX conformation, and reduced its MOM translocation and integration; their exposure of the BAX alpha1-alpha2 loop allosterically sequestered its alpha9 membrane anchor in the groove. The crystal structure of an alpha6 mutant revealed additional allosteric effects. The results suggest that the alpha1 and alpha6 region drives MOM association and integration, whereas groove binding favors subsequent steps toward oligomerization. | ||
| + | |||
| + | BAX Activation: Mutations Near Its Proposed Non-canonical BH3 Binding Site Reveal Allosteric Changes Controlling Mitochondrial Association.,Dengler MA, Robin AY, Gibson L, Li MX, Sandow JJ, Iyer S, Webb AI, Westphal D, Dewson G, Adams JM Cell Rep. 2019 Apr 9;27(2):359-373.e6. doi: 10.1016/j.celrep.2019.03.040. PMID:30970242<ref>PMID:30970242</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6eb6" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Robin, A Y]] | [[Category: Robin, A Y]] | ||
Revision as of 07:50, 24 April 2019
Crystal structure of BAX W139A monomer
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