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Open data
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Basic information
Entry | ![]() |
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![]() | Antiapoptotic membrane protein, (DpV84gp022) Deerpox virus
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Function / homology | Poxvirus F1/C10 / Apoptosis regulator M11L like / symbiont-mediated suppression of host apoptosis / Bcl-2-like superfamily / regulation of apoptotic process / membrane / Antiapoptotic membrane protein![]() |
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![]() | ![]() Title: Structural basis of Deerpox virus-mediated inhibition of apoptosis. Authors: Denis R Burton / Sofia Caria / Bevan Marshall / Michele Barry / Marc Kvansakul / ![]() ![]() Abstract: 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 ...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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Structure visualization
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Downloads & links
-Data source
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-Related structure data
Related structure data | ![]() 4uf1C ![]() 4uf2C ![]() 4uf3C C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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External links
Related items in Molecule of the Month |
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-Models
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Sample
![]() | Name: Antiapoptotic membrane protein, (DpV84gp022) Deerpox virus Specimen concentration: 0.22-6.34 |
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Buffer | Name: HEPES / Concentration: 25.00 mM / pH: 7.5 / Composition: 150 mM NaCl |
Entity #186 | Type: protein / Description: Antiapoptotic membrane protein / Formula weight: 19.6 / Num. of mol.: 2 / Source: Deerpox virus W-1170-84 / References: UniProt: Q08FF8 Sequence: MGSSHHHHHH SQDMEAAIEF DEIVKKLLNI YINDICTTGE KRLLNNYEKS ILDRIYKSCE YIKKNYELDF NSMYNQININ DITTSDIKSK IIEALLIDSR PSVKLATLSF ISLIAEKWGE KNRAKIMEIL SNEIVEKISN NGKDFIDFID RDDDDIVDDY VLITNYLK |
-Experimental information
Beam | Instrument name: Australian Synchrotron SAXS/WAXS / City: Melbourne / 国: Australia ![]() | ||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 1M | ||||||||||||||||||||||||||||||
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