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| | <StructureSection load='2vof' size='340' side='right'caption='[[2vof]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='2vof' size='340' side='right'caption='[[2vof]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vof]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VOF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VOF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vof]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VOF FirstGlance]. <br> |
| | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| | <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> | | <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> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vog|2vog]], [[2voh|2voh]], [[2voi|2voi]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vog|2vog]], [[2voh|2voh]], [[2voi|2voi]]</div></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2vof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vof OCA], [http://pdbe.org/2vof PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vof RCSB], [http://www.ebi.ac.uk/pdbsum/2vof PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vof ProSAT]</span></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=2vof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vof OCA], [https://pdbe.org/2vof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vof RCSB], [https://www.ebi.ac.uk/pdbsum/2vof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vof ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BBC3_MOUSE BBC3_MOUSE]] Essential mediator of p53/TP53-dependent and p53/TP53-independent apoptosis (By similarity). Regulates ER stress-induced neuronal apoptosis.<ref>PMID:21159964</ref> <ref>PMID:22761832</ref> | + | [[https://www.uniprot.org/uniprot/BBC3_MOUSE BBC3_MOUSE]] Essential mediator of p53/TP53-dependent and p53/TP53-independent apoptosis (By similarity). Regulates ER stress-induced neuronal apoptosis.<ref>PMID:21159964</ref> <ref>PMID:22761832</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Structural highlights
Function
[BBC3_MOUSE] Essential mediator of p53/TP53-dependent and p53/TP53-independent apoptosis (By similarity). Regulates ER stress-induced neuronal apoptosis.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Apoptotic pathways are regulated by protein-protein interactions. Interaction of the BH3 domains of proapoptotic Bcl-2 family proteins with the hydrophobic groove of prosurvival proteins is critical. Whereas some BH3 domains bind in a promiscuous manner, others exhibit considerable selectivity and the sequence characteristics that distinguish these activities are unclear. In this study, crystal structures of complexes between the prosurvival protein A1 and the BH3 domains from Puma, Bmf, Bak, and Bid have been solved. The structure of A1 is similar to that of other prosurvival proteins, although features, such as an acidic patch in the binding groove, may allow specific therapeutic modulation of apoptosis. Significant conformational plasticity was observed in the intermolecular interactions and these differences explain some of the variation in affinity. This study, in combination with published data, suggests that interactions between conserved residues demarcate optimal binding.
Structural plasticity underpins promiscuous binding of the prosurvival protein A1.,Smits C, Czabotar PE, Hinds MG, Day CL Structure. 2008 May;16(5):818-29. PMID:18462686[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Galehdar Z, Swan P, Fuerth B, Callaghan SM, Park DS, Cregan SP. Neuronal apoptosis induced by endoplasmic reticulum stress is regulated by ATF4-CHOP-mediated induction of the Bcl-2 homology 3-only member PUMA. J Neurosci. 2010 Dec 15;30(50):16938-48. doi: 10.1523/JNEUROSCI.1598-10.2010. PMID:21159964 doi:http://dx.doi.org/10.1523/JNEUROSCI.1598-10.2010
- ↑ Ghosh AP, Klocke BJ, Ballestas ME, Roth KA. CHOP potentially co-operates with FOXO3a in neuronal cells to regulate PUMA and BIM expression in response to ER stress. PLoS One. 2012;7(6):e39586. doi: 10.1371/journal.pone.0039586. Epub 2012 Jun 28. PMID:22761832 doi:http://dx.doi.org/10.1371/journal.pone.0039586
- ↑ Smits C, Czabotar PE, Hinds MG, Day CL. Structural plasticity underpins promiscuous binding of the prosurvival protein A1. Structure. 2008 May;16(5):818-29. PMID:18462686 doi:http://dx.doi.org/10.1016/j.str.2008.02.009
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