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| | <StructureSection load='4b4s' size='340' side='right'caption='[[4b4s]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='4b4s' size='340' side='right'caption='[[4b4s]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4b4s]] is a 2 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=4B4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B4S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4b4s]] is a 2 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=4B4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B4S FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2v6q|2v6q]], [[2vm6|2vm6]], [[2wh6|2wh6]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=4b4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b4s OCA], [https://pdbe.org/4b4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b4s RCSB], [https://www.ebi.ac.uk/pdbsum/4b4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b4s 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=4b4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b4s OCA], [https://pdbe.org/4b4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b4s RCSB], [https://www.ebi.ac.uk/pdbsum/4b4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b4s ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/B2L10_HUMAN B2L10_HUMAN]] Promotes cell survival. Suppresses apoptosis induced by BAX but not BAK.<ref>PMID:11278245</ref> [[https://www.uniprot.org/uniprot/B2L11_HUMAN B2L11_HUMAN]] Induces apoptosis and anoikis. Isoform BimL is more potent than isoform BimEL. Isoform Bim-alpha1, isoform Bim-alpha2 and isoform Bim-alpha3 induce apoptosis, although less potent than isoform BimEL, isoform BimL and isoform BimS. Isoform Bim-gamma induces apoptosis. Isoform Bim-alpha3 induces apoptosis possibly through a caspase-mediated pathway. Isoform BimAC and isoform BimABC lack the ability to induce apoptosis.<ref>PMID:9430630</ref> <ref>PMID:11734221</ref> <ref>PMID:12019181</ref> <ref>PMID:11997495</ref> <ref>PMID:15147734</ref> <ref>PMID:15486195</ref>
| + | [https://www.uniprot.org/uniprot/B2L10_HUMAN B2L10_HUMAN] Promotes cell survival. Suppresses apoptosis induced by BAX but not BAK.<ref>PMID:11278245</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hinds, M G]] | + | [[Category: Hinds MG]] |
| - | [[Category: Kvansakul, M]] | + | [[Category: Kvansakul M]] |
| - | [[Category: Rautureau, G J.P]] | + | [[Category: Rautureau GJP]] |
| - | [[Category: Apoptosis]]
| + | |
| Structural highlights
Function
B2L10_HUMAN Promotes cell survival. Suppresses apoptosis induced by BAX but not BAK.[1]
Publication Abstract from PubMed
B-cell lymphoma-2 (Bcl-2) proteins mediate intrinsic-, or mitochondrial-, initiated apoptosis. We have investigated the structure and function of the least characterized Bcl-2 family member, Bcl-B, solving the crystal structure of a Bcl-B:Bim complex to 1.9 A resolution. Bcl-B is distinguished from other Bcl-2 family members through an insertion of an unstructured loop between helices alpha5 and alpha6. Probing Bcl-B interactions with Bcl-2 homology (BH)3 motifs using a combination of biophysical- and cell-based assays revealed a unique BH3-only protein binding profile. Bcl-B has high-affinity interactions with Bim and Bik only. Our results not only delineate the mode of action of Bcl-B but also complete our understanding of the specific interactions between BH3-only proteins and their prosurvival Bcl-2 counterparts. Notably, we conclude that Bim is the universal prosurvival antagonist as no other BH3-only protein binds all six prosurvival proteins and that Mcl-1 and Bcl-x(L) form a distinct prosurvival dyad.
The restricted binding repertoire of Bcl-B leaves Bim as the universal BH3-only prosurvival Bcl-2 protein antagonist.,Rautureau GJ, Yabal M, Yang H, Huang DC, Kvansakul M, Hinds MG Cell Death Dis. 2012 Dec 13;3:e443. doi: 10.1038/cddis.2012.178. PMID:23235460[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ke N, Godzik A, Reed JC. Bcl-B, a novel Bcl-2 family member that differentially binds and regulates Bax and Bak. J Biol Chem. 2001 Apr 20;276(16):12481-4. Epub 2001 Feb 21. PMID:11278245 doi:http://dx.doi.org/10.1074/jbc.C000871200
- ↑ Rautureau GJ, Yabal M, Yang H, Huang DC, Kvansakul M, Hinds MG. The restricted binding repertoire of Bcl-B leaves Bim as the universal BH3-only prosurvival Bcl-2 protein antagonist. Cell Death Dis. 2012 Dec 13;3:e443. doi: 10.1038/cddis.2012.178. PMID:23235460 doi:http://dx.doi.org/10.1038/cddis.2012.178
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