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4k5a

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Revision as of 02:23, 5 August 2016

Co-crystallization with conformation-specific designed ankyrin repeat proteins explains the conformational flexibility of BCL-W

Structural highlights

4k5a is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895 and Bovin. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	4k5b
Gene:	BCL2L2 (BOVIN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[B2CL2_BOVIN] Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX (By similarity).

Publication Abstract from PubMed

BCL-W is a member of the BCL-2 family of anti-apoptotic proteins. A key event in the regulation of apoptosis is the heterodimerization between anti-apoptotic and pro-apoptotic family members, which involves a conserved surface-exposed groove on the anti-apoptotic proteins. Crystal structures of the ligand binding-competent conformation exist for all anti-apoptotic family members, with the exception of BCL-W, due to the flexibility of the BCL-W groove region. Existing structures had suggested major deviations of the BCL-W groove region from the otherwise structurally highly related remaining anti-apoptotic family members. To capture its ligand binding-competent conformation by counteracting the conformational flexibility of the BCL-W groove, we had selected high-affinity groove-binding designed ankyrin repeat proteins (DARPins) using ribosome-display. We now determined two high-resolution crystal structures of human BCL-W in complex with different DARPins at a resolution of 1.5 and 1.85A, in which the structure of BCL-W is virtually identical, and in both structures BCL-W adopts a conformation extremely similar to the ligand-free conformation of its closest relative BCL-XL. However, distinct differences to all previous BCL-W structures are evident, notably in the ligand-binding region. We provide the first structural explanation for the conformational flexibility of the BCL-W groove region in comparison to other BCL-2 family members. Due to the importance of the anti-apoptotic BCL-2 family as drug targets, the presented crystal structure of ligand binding-competent BCL-W may serve as a valuable basis for structure-based drug design in the future and provides a missing piece for the structural characterization of this protein family.

Co-crystallization with conformation-specific designed ankyrin repeat proteins explains the conformational flexibility of BCL-W.,Schilling J, Schoppe J, Sauer E, Pluckthun A J Mol Biol. 2014 Apr 17. pii: S0022-2836(14)00194-6. doi:, 10.1016/j.jmb.2014.04.010. PMID:24747052^[1]

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

References

↑ Schilling J, Schoppe J, Sauer E, Pluckthun A. Co-crystallization with conformation-specific designed ankyrin repeat proteins explains the conformational flexibility of BCL-W. J Mol Biol. 2014 Apr 17. pii: S0022-2836(14)00194-6. doi:, 10.1016/j.jmb.2014.04.010. PMID:24747052 doi:http://dx.doi.org/10.1016/j.jmb.2014.04.010

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4k5a"

@@ Line 1: / Line 1: @@
 ==Co-crystallization with conformation-specific designed ankyrin repeat proteins explains the conformational flexibility of BCL-W==
 <StructureSection load='4k5a' size='340' side='right' caption='[[4k5a]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4k5b|4k5b]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BCL2L2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4k5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k5a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k5a RCSB], [http://www.ebi.ac.uk/pdbsum/4k5a PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4k5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k5a OCA], [http://pdbe.org/4k5a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k5a RCSB], [http://www.ebi.ac.uk/pdbsum/4k5a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k5a ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4k5a" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4k5a

From Proteopedia

Revision as of 02:23, 5 August 2016

Co-crystallization with conformation-specific designed ankyrin repeat proteins explains the conformational flexibility of BCL-W

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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