4b4s
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of a pro-survival Bcl-2:Bim BH3 complex== | |
| + | <StructureSection load='4b4s' size='340' side='right'caption='[[4b4s]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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='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='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> | ||
| + | </table> | ||
| + | == 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:23235460</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4b4s" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Hinds MG]] | ||
| + | [[Category: Kvansakul M]] | ||
| + | [[Category: Rautureau GJP]] | ||
Current revision
Crystal Structure of a pro-survival Bcl-2:Bim BH3 complex
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