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4uf2

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==Deerpox virus DPV022 in complex with Bax BH3==
==Deerpox virus DPV022 in complex with Bax BH3==
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<StructureSection load='4uf2' size='340' side='right' caption='[[4uf2]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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<StructureSection load='4uf2' size='340' side='right'caption='[[4uf2]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4uf2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UF2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UF2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4uf2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Deerpox_virus_W-1170-84 Deerpox virus W-1170-84] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UF2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UF2 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uf1|4uf1]], [[4uf3|4uf3]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<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=4uf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uf2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uf2 RCSB], [http://www.ebi.ac.uk/pdbsum/4uf2 PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4uf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uf2 OCA], [https://pdbe.org/4uf2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uf2 RCSB], [https://www.ebi.ac.uk/pdbsum/4uf2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uf2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/BAX_HUMAN BAX_HUMAN]] Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis.<ref>PMID:8358790</ref> <ref>PMID:10772918</ref> <ref>PMID:8521816</ref> <ref>PMID:16113678</ref> <ref>PMID:18948948</ref> <ref>PMID:21199865</ref>
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[https://www.uniprot.org/uniprot/DPV22_DPV83 DPV22_DPV83] Plays a role in the inhibition of host apoptosis by sequestering and inactivating several proapoptotic BCL-2 proteins, including BAK1 and BAX. Prevents the conformational activation of both of them.<ref>PMID:21159883</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Apoptosis is a key innate defence mechanism to eliminate virally infected cells. To counteract premature host-cell apoptosis, poxviruses have evolved numerous molecular strategies, including the use of Bcl-2 proteins, to ensure their own survival. Here, it is reported that the Deerpox virus inhibitor of apoptosis, DPV022, only engages a highly restricted set of death-inducing Bcl-2 proteins, including Bim, Bax and Bak, with modest affinities. Structural analysis reveals that DPV022 adopts a Bcl-2 fold with a dimeric domain-swapped topology and binds pro-death Bcl-2 proteins via two conserved ligand-binding grooves found on opposite sides of the dimer. Structures of DPV022 bound to Bim, Bak and Bax BH3 domains reveal that a partial obstruction of the binding groove is likely to be responsible for the modest affinities of DPV022 for BH3 domains. These findings reveal that domain-swapped dimeric Bcl-2 folds are not unusual and may be found more widely in viruses. Furthermore, the modest affinities of DPV022 for pro-death Bcl-2 proteins suggest that two distinct classes of anti-apoptotic viral Bcl-2 proteins exist: those that are monomeric and tightly bind a range of death-inducing Bcl-2 proteins, and others such as DPV022 that are dimeric and only bind a very limited number of death-inducing Bcl-2 proteins with modest affinities.
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Structural basis of Deerpox virus-mediated inhibition of apoptosis.,Burton DR, Caria S, Marshall B, Barry M, Kvansakul M Acta Crystallogr D Biol Crystallogr. 2015 Aug 1;71(Pt 8):1593-603. doi:, 10.1107/S1399004715009402. Epub 2015 Jul 28. PMID:26249341<ref>PMID:26249341</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Burton, D R]]
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[[Category: Deerpox virus W-1170-84]]
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[[Category: Kvansakul, M]]
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[[Category: Homo sapiens]]
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[[Category: Apoptosis]]
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[[Category: Large Structures]]
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[[Category: Bax bh3]]
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[[Category: Burton DR]]
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[[Category: Bcl-2]]
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[[Category: Kvansakul M]]
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[[Category: Deerpox virus]]
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[[Category: Viral protein]]
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Current revision

Deerpox virus DPV022 in complex with Bax BH3

PDB ID 4uf2

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