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2y6w

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Revision as of 12:24, 27 April 2022

Structure of a Bcl-w dimer

Structural highlights

2y6w is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1o0l, 1zy3, 1mk3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[B2CL2_HUMAN] Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX.^[1]

Publication Abstract from PubMed

The prosurvival and proapoptotic proteins of the BCL-2 family share a similar three-dimensional fold despite their opposing functions. However, many biochemical studies highlight the requirement for conformational changes for the functioning of both types of proteins, although structural data to support such changes remain elusive. Here, we describe the X-ray structure of dimeric BCL-W that reveals a major conformational change involving helices alpha3 and alpha4 hinging away from the core of the protein. Biochemical and functional studies reveal that the alpha4-alpha5 hinge region is required for dimerization of BCL-W, and functioning of both pro- and antiapoptotic BCL-2 proteins. Hence, this structure reveals a conformational flexibility not seen in previous BCL-2 protein structures and provides insights into how these regulators of apoptosis can change conformation to exert their function.

Crystal Structure of a BCL-W Domain-Swapped Dimer: Implications for the Function of BCL-2 Family Proteins.,Lee EF, Dewson G, Smith BJ, Evangelista M, Pettikiriarachchi A, Dogovski C, Perugini MA, Colman PM, Fairlie WD Structure. 2011 Oct 12;19(10):1467-76. PMID:22000515^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
↑ Lee EF, Dewson G, Smith BJ, Evangelista M, Pettikiriarachchi A, Dogovski C, Perugini MA, Colman PM, Fairlie WD. Crystal Structure of a BCL-W Domain-Swapped Dimer: Implications for the Function of BCL-2 Family Proteins. Structure. 2011 Oct 12;19(10):1467-76. PMID:22000515 doi:10.1016/j.str.2011.07.015

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2y6w"

@@ Line 3: / Line 3: @@
 <StructureSection load='2y6w' size='340' side='right'caption='[[2y6w]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2y6w]] is a 2 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=2Y6W OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2Y6W FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2y6w]] 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=2Y6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y6W FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1o0l|1o0l]], [[1zy3|1zy3]], [[1mk3|1mk3]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1o0l|1o0l]], [[1zy3|1zy3]], [[1mk3|1mk3]]</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=2y6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y6w OCA], [http://pdbe.org/2y6w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2y6w RCSB], [http://www.ebi.ac.uk/pdbsum/2y6w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2y6w 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=2y6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y6w OCA], [https://pdbe.org/2y6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y6w RCSB], [https://www.ebi.ac.uk/pdbsum/2y6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y6w ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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/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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

2y6w

From Proteopedia

Revision as of 12:24, 27 April 2022

Structure of a Bcl-w dimer

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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