3jrv: Difference between revisions

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</table>

== Function ==

[https://www.uniprot.org/uniprot/~~K7_VACCW K7_VACCW~~] Bcl-2-like protein which, through its interaction with the DEAD box RNA helicase DDX3X/DDX3, prevents TBK1/IKKepsilon-mediated IRF3 activation. Contributes to virulence by binding to the host TRAF6 and IRAK2 and preventing host NF-kappa-B activation.

[https://www.uniprot.org/uniprot/PG044_VACCW PG044_VACCW] Virulence factor that affects the acute immune response to infection (PubMed:23580427). Bcl-2-like protein which, through its interaction with the DEAD box RNA helicase DDX3X/DDX3, prevents TBK1/IKKepsilon-mediated IRF3 activation. Contributes to virulence by binding to the host TRAF6 and IRAK2 and preventing host NF-kappa-B activation.<ref>PMID:18636090</ref> <ref>PMID:19913487</ref> <ref>PMID:23580427</ref>

== Publication Abstract from PubMed ==

Poxviruses are DNA viruses that express numerous proteins to subvert the host immune response. Vaccinia virus protein K7 adopts a Bcl-2 fold and displays structural and functional similarities to Toll-like receptor antagonist A52. Both proteins interact with IRAK2 and TRAF6 and suppress TLR-dependent NF-kappaB activation. However, unlike A52, K7 also forms a complex with RNA helicase DDX3 and antagonizes interferon-beta promoter induction. We have narrowed the K7 binding site to an N-terminal peptide motif of DDX3 ahead of its core RNA-helicase domains. The crystal structure of full-length K7 in complex with the DDX3 peptide reveals a thumblike projection of tandem phenalyalanine residues of DDX3 into a deep hydrophobic cleft. Mutagenesis of these phenylalanines abolishes the effects of DDX3 on interferon-beta promoter induction. The structure of K7-DDX3 reveals a novel binding mode by a viral Bcl-2 protein that antagonizes a key pathway in innate immunity.

Structural basis for targeting of human RNA helicase DDX3 by poxvirus protein K7.,Oda S, Schroder M, Khan AR Structure. 2009 Nov 11;17(11):1528-37. PMID:19913487<ref>PMID:19913487</ref>

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

</div>

==See Also==

*[[Helicase 3D structures|Helicase 3D structures]]

== References ==

__TOC__

</StructureSection>

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 </table>
 == Function ==
-[https://www.uniprot.org/uniprot/K7_VACCW K7_VACCW] Bcl-2-like protein which, through its interaction with the DEAD box RNA helicase DDX3X/DDX3, prevents TBK1/IKKepsilon-mediated IRF3 activation. Contributes to virulence by binding to the host TRAF6 and IRAK2 and preventing host NF-kappa-B activation.
+[https://www.uniprot.org/uniprot/PG044_VACCW PG044_VACCW] Virulence factor that affects the acute immune response to infection (PubMed:23580427). Bcl-2-like protein which, through its interaction with the DEAD box RNA helicase DDX3X/DDX3, prevents TBK1/IKKepsilon-mediated IRF3 activation. Contributes to virulence by binding to the host TRAF6 and IRAK2 and preventing host NF-kappa-B activation.<ref>PMID:18636090</ref> <ref>PMID:19913487</ref> <ref>PMID:23580427</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Poxviruses are DNA viruses that express numerous proteins to subvert the host immune response. Vaccinia virus protein K7 adopts a Bcl-2 fold and displays structural and functional similarities to Toll-like receptor antagonist A52. Both proteins interact with IRAK2 and TRAF6 and suppress TLR-dependent NF-kappaB activation. However, unlike A52, K7 also forms a complex with RNA helicase DDX3 and antagonizes interferon-beta promoter induction. We have narrowed the K7 binding site to an N-terminal peptide motif of DDX3 ahead of its core RNA-helicase domains. The crystal structure of full-length K7 in complex with the DDX3 peptide reveals a thumblike projection of tandem phenalyalanine residues of DDX3 into a deep hydrophobic cleft. Mutagenesis of these phenylalanines abolishes the effects of DDX3 on interferon-beta promoter induction. The structure of K7-DDX3 reveals a novel binding mode by a viral Bcl-2 protein that antagonizes a key pathway in innate immunity.
+Structural basis for targeting of human RNA helicase DDX3 by poxvirus protein K7.,Oda S, Schroder M, Khan AR Structure. 2009 Nov 11;17(11):1528-37. PMID:19913487<ref>PMID:19913487</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3jrv" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Helicase 3D structures|Helicase 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>