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| | ==Structural model of complex of Bcl-w protein with Bid BH3-peptide== | | ==Structural model of complex of Bcl-w protein with Bid BH3-peptide== |
| - | <StructureSection load='1zy3' size='340' side='right'caption='[[1zy3]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='1zy3' size='340' side='right'caption='[[1zy3]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1zy3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZY3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZY3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1zy3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZY3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZY3 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mk3|1mk3]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1zy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zy3 OCA], [https://pdbe.org/1zy3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zy3 RCSB], [https://www.ebi.ac.uk/pdbsum/1zy3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zy3 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=1zy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zy3 OCA], [https://pdbe.org/1zy3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zy3 RCSB], [https://www.ebi.ac.uk/pdbsum/1zy3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zy3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/B2CL2_HUMAN B2CL2_HUMAN]] Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX.<ref>PMID:8761287</ref> [[https://www.uniprot.org/uniprot/BID_HUMAN BID_HUMAN]] The major proteolytic product p15 BID allows the release of cytochrome c (By similarity). Isoform 1, isoform 2 and isoform 4 induce ICE-like proteases and apoptosis. Isoform 3 does not induce apoptosis. Counters the protective effect of Bcl-2.<ref>PMID:14583606</ref>
| + | [https://www.uniprot.org/uniprot/B2CL2_HUMAN B2CL2_HUMAN] Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX.<ref>PMID:8761287</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Denisov, A Y]] | + | [[Category: Denisov AY]] |
| - | [[Category: Gehring, K]] | + | [[Category: Gehring K]] |
| - | [[Category: Apoptosis]]
| + | |
| - | [[Category: Bcl-w]]
| + | |
| - | [[Category: Bh3-peptide]]
| + | |
| Structural highlights
Function
B2CL2_HUMAN Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX.[1]
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
A peptide corresponding to the BH3 region of the proapoptotic protein, BID, could be bound in the cleft of the antiapoptotic protein, BCL-w. This binding induced major conformational rearrangements in both the peptide and protein components of the complex and led to the displacement and unfolding of the BCL-w C-terminal alpha-helix. The structure of BCL-w with a bound BID-BH3 peptide was determined using NMR spectroscopy and molecular docking. These studies confirmed that a region of 16 residues of the BID-BH3 peptide is responsible for its strong binding to BCL-w and BCL-x(L). The interactions of BCL-w and the BID-BH3 peptide complex with dodecylphosphocholine micelles were characterized and showed that the conformational change of BCL-w upon lipid binding occurred at the same time as the release and unfolding of the BH3 peptide.
Structural model of the BCL-w-BID peptide complex and its interactions with phospholipid micelles.,Denisov AY, Chen G, Sprules T, Moldoveanu T, Beauparlant P, Gehring K Biochemistry. 2006 Feb 21;45(7):2250-6. PMID:16475813[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gibson L, Holmgreen SP, Huang DC, Bernard O, Copeland NG, Jenkins NA, Sutherland GR, Baker E, Adams JM, Cory S. bcl-w, a novel member of the bcl-2 family, promotes cell survival. Oncogene. 1996 Aug 15;13(4):665-75. PMID:8761287
- ↑ Denisov AY, Chen G, Sprules T, Moldoveanu T, Beauparlant P, Gehring K. Structural model of the BCL-w-BID peptide complex and its interactions with phospholipid micelles. Biochemistry. 2006 Feb 21;45(7):2250-6. PMID:16475813 doi:10.1021/bi052332s
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