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Open data
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Basic information
Entry | Database: SASBDB / ID: SASDBV4 |
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![]() | Vaccinia virus MVA F1L antiapoptotic Bcl-2 viral protein
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Function / homology | ![]() : / host cell mitochondrial outer membrane / : / regulation of apoptotic process / ![]() Similarity search - Function |
Biological species | ![]() ![]() ![]() |
![]() | ![]() Title: The N Terminus of the Vaccinia Virus Protein F1L Is an Intrinsically Unstructured Region That Is Not Involved in Apoptosis Regulation. Authors: Sofia Caria / Bevan Marshall / Robyn-Lee Burton / Stephanie Campbell / Delara Pantaki-Eimany / Christine J Hawkins / Michele Barry / Marc Kvansakul / ![]() ![]() Abstract: Subversion of host cell apoptotic responses is a prominent feature of viral immune evasion strategies to prevent premature clearance of infected cells. Numerous poxviruses encode structural and ...Subversion of host cell apoptotic responses is a prominent feature of viral immune evasion strategies to prevent premature clearance of infected cells. Numerous poxviruses encode structural and functional homologs of the Bcl-2 family of proteins, and vaccinia virus harbors antiapoptotic F1L that potently inhibits the mitochondrial apoptotic checkpoint. Recently F1L has been assigned a caspase-9 inhibitory function attributed to an N-terminal α helical region of F1L spanning residues 1-15 (1) preceding the domain-swapped Bcl-2-like domains. Using a reconstituted caspase inhibition assay in yeast we found that unlike AcP35, a well characterized caspase-9 inhibitor from the insect virus Autographa californica multiple nucleopolyhedrovirus, F1L does not prevent caspase-9-mediated yeast cell death. Furthermore, we found that deletion of the F1L N-terminal region does not impede F1L antiapoptotic activity in the context of a viral infection. Solution analysis of the F1L N-terminal regions using small angle x-ray scattering indicates that the region of F1L spanning residues 1-50 located N-terminally from the Bcl-2 fold is an intrinsically unstructured region. We conclude that the N terminus of F1L is not involved in apoptosis inhibition and may act as a regulatory element in other signaling pathways in a manner reminiscent of other unstructured regulatory elements commonly found in mammalian prosurvival Bcl-2 members including Bcl-xL and Mcl-1. |
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Structure visualization
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Downloads & links
-Data source
SASBDB page | ![]() |
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-Related structure data
Similar structure data |
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External links
Related items in Molecule of the Month |
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-Models
Model #535 | ![]() Type: mix / Software: BUNCH / Radius of dummy atoms: 1.90 A / Chi-square value: 7.29 ![]() |
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Model #536 | ![]() Type: mix / Software: CORAL / Radius of dummy atoms: 1.90 A / Chi-square value: 3.8416 ![]() |
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Sample
![]() | Name: Vaccinia virus MVA F1L antiapoptotic Bcl-2 viral protein Specimen concentration: 0.12-3.60 |
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Buffer | Name: 25 mM HEPES, 150 mM NaCl, 5 mM DTT / pH: 7.5 |
Entity #341 | Name: MVA F1L (Protein F1) / Type: protein / Description: MVA F1L antiapoptotic Bcl-2 viral protein / Formula weight: 25.291 / Num. of mol.: 2 / Source: Vaccinia virus / References: UniProt: O57173 Sequence: MGSSHHHHHH SQDPMLSMFM CNNIVDYVDG IVQDIEDEAS NNVDHDYVYP LPENMVYRFD KSTNILDYLS TERDHVMMAV RYYMSKQRLD DLYRQLPTKT RSYIDIINIY CDKVSNDYNR DMNIMYDMAS TKSFTVYDIN NEVNTILMDN KGLGVRLATI SFITELGRRC ...Sequence: MGSSHHHHHH SQDPMLSMFM CNNIVDYVDG IVQDIEDEAS NNVDHDYVYP LPENMVYRFD KSTNILDYLS TERDHVMMAV RYYMSKQRLD DLYRQLPTKT RSYIDIINIY CDKVSNDYNR DMNIMYDMAS TKSFTVYDIN NEVNTILMDN KGLGVRLATI SFITELGRRC MNPVKTIKMF TLLSHTICDD CFVDYITDIS PPDNTIPNTS TREYLK |
-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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