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4uf3

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Deerpox virus DPV022 in complex with Bim BH3

Structural highlights

4uf3 is a 2 chain structure with sequence from Deerpox virus W-1170-84 and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.7Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1]

Publication Abstract from PubMed

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.

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^[2]

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

References

↑ Banadyga L, Lam SC, Okamoto T, Kvansakul M, Huang DC, Barry M. Deerpox virus encodes an inhibitor of apoptosis that regulates Bak and Bax. J Virol. 2011 Mar;85(5):1922-34. PMID:21159883 doi:10.1128/JVI.01959-10
↑ Burton DR, Caria S, Marshall B, Barry M, Kvansakul M. Structural basis of Deerpox virus-mediated inhibition of apoptosis. Acta Crystallogr D Biol Crystallogr. 2015 Aug 1;71(Pt 8):1593-603. doi:, 10.1107/S1399004715009402. Epub 2015 Jul 28. PMID:26249341 doi:http://dx.doi.org/10.1107/S1399004715009402

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/4uf3"

Categories: Deerpox virus W-1170-84 | Homo sapiens | Large Structures | Burton DR | Kvansakul M

@@ Line 1: / Line 1: @@
 ==Deerpox virus DPV022 in complex with Bim BH3==
-<StructureSection load='4uf3' size='340' side='right' caption='[[4uf3]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+<StructureSection load='4uf3' size='340' side='right'caption='[[4uf3]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4uf3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UF3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UF3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4uf3]] 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=4UF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UF3 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uf1|4uf1]], [[4uf2|4uf2]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</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=4uf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uf3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uf3 RCSB], [http://www.ebi.ac.uk/pdbsum/4uf3 PDBsum]</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=4uf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uf3 OCA], [https://pdbe.org/4uf3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uf3 RCSB], [https://www.ebi.ac.uk/pdbsum/4uf3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uf3 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/B2L11_HUMAN B2L11_HUMAN]] Induces apoptosis and anoikis. Isoform BimL is more potent than isoform BimEL. Isoform Bim-alpha1, isoform Bim-alpha2 and isoform Bim-alpha3 induce apoptosis, although less potent than isoform BimEL, isoform BimL and isoform BimS. Isoform Bim-gamma induces apoptosis. Isoform Bim-alpha3 induces apoptosis possibly through a caspase-mediated pathway. Isoform BimAC and isoform BimABC lack the ability to induce apoptosis.<ref>PMID:9430630</ref> <ref>PMID:11734221</ref> <ref>PMID:12019181</ref> <ref>PMID:11997495</ref> <ref>PMID:15147734</ref> <ref>PMID:15486195</ref>
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4uf3" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Burton, D R]]
+[[Category: Deerpox virus W-1170-84]]
-[[Category: Kvansakul, M]]
+[[Category: Homo sapiens]]
-[[Category: Apoptosis]]
+[[Category: Large Structures]]
-[[Category: Bcl-2]]
+[[Category: Burton DR]]
-[[Category: Bim bh3]]
+[[Category: Kvansakul M]]
-[[Category: Deerpox virus]]
-[[Category: Dpv022]]
-[[Category: Viral protein]]

4uf3

From Proteopedia

Current revision

Deerpox virus DPV022 in complex with Bim BH3

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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