4hlx: Difference between revisions
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== | ==The crystal structure of the DNA binding domain of vIRF-1 from the oncogenic KSHV== | ||
[[4hlx]] is a 4 chain structure with sequence from [ | <StructureSection load='4hlx' size='340' side='right'caption='[[4hlx]], [[Resolution|resolution]] 2.38Å' scene=''> | ||
[[ | == Structural highlights == | ||
[[Category: | <table><tr><td colspan='2'>[[4hlx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_gammaherpesvirus_8 Human gammaherpesvirus 8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HLX FirstGlance]. <br> | ||
[[Category: | </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=4hlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hlx OCA], [https://pdbe.org/4hlx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hlx RCSB], [https://www.ebi.ac.uk/pdbsum/4hlx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hlx ProSAT]</span></td></tr> | ||
[[Category: | </table> | ||
[[Category: | == Function == | ||
[https://www.uniprot.org/uniprot/Q77Q82_HHV8 Q77Q82_HHV8] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Kaposi's sarcoma-associated herpesvirus encodes four viral homologues to cellular interferon regulatory factors (IRFs), where the most studied is vIRF-1. Even though vIRF-1 shows sequence homology to the N-terminal DNA-binding domain (DBD) of human IRFs, a specific role for this domain in vIRF-1's function has remained uncertain. To provide insights into the function of the vIRF-1 DBD, we have determined the crystal structure of it in complex with DNA and in its apo-form. Using a thermal stability shift assay (TSSA), we show that the vIRF-1 DBD binds DNA, whereas full-length vIRF-1 does not, suggesting a cis-acting regulatory mechanism in similarity to human IRFs. The complex structure of vIRF-1 DBD reveals interactions with the DNA backbone and the positioning of two arginines for specific recognition in the major grove. A superimposition with human IRF-3 reveals a similar positioning of the two specificity-determining arginines, and additional TSSAs indicate binding of vIRF-1 to an IRF-3 operator consensus sequence. The results from this study, therefore, provide support that vIRF-1 has evolved to bind DNA and plays a role in DNA binding in the context of transcriptional regulation and might act on some of the many operator sequences controlled by human IRF-3. | |||
The crystal structure of the DNA-binding domain of vIRF-1 from the oncogenic KSHV reveals a conserved fold for DNA binding and reinforces its role as a transcription factor.,Hew K, Dahlroth SL, Venkatachalam R, Nasertorabi F, Lim BT, Cornvik T, Nordlund P Nucleic Acids Res. 2013 Feb 21. PMID:23435230<ref>PMID:23435230</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4hlx" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Interferon regulatory factor|Interferon regulatory factor]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human gammaherpesvirus 8]] | |||
[[Category: Large Structures]] | |||
[[Category: Hew K]] | |||
[[Category: Venkatachalam R]] | |||
Latest revision as of 11:25, 3 November 2022
The crystal structure of the DNA binding domain of vIRF-1 from the oncogenic KSHVThe crystal structure of the DNA binding domain of vIRF-1 from the oncogenic KSHV
Structural highlights
FunctionPublication Abstract from PubMedKaposi's sarcoma-associated herpesvirus encodes four viral homologues to cellular interferon regulatory factors (IRFs), where the most studied is vIRF-1. Even though vIRF-1 shows sequence homology to the N-terminal DNA-binding domain (DBD) of human IRFs, a specific role for this domain in vIRF-1's function has remained uncertain. To provide insights into the function of the vIRF-1 DBD, we have determined the crystal structure of it in complex with DNA and in its apo-form. Using a thermal stability shift assay (TSSA), we show that the vIRF-1 DBD binds DNA, whereas full-length vIRF-1 does not, suggesting a cis-acting regulatory mechanism in similarity to human IRFs. The complex structure of vIRF-1 DBD reveals interactions with the DNA backbone and the positioning of two arginines for specific recognition in the major grove. A superimposition with human IRF-3 reveals a similar positioning of the two specificity-determining arginines, and additional TSSAs indicate binding of vIRF-1 to an IRF-3 operator consensus sequence. The results from this study, therefore, provide support that vIRF-1 has evolved to bind DNA and plays a role in DNA binding in the context of transcriptional regulation and might act on some of the many operator sequences controlled by human IRF-3. The crystal structure of the DNA-binding domain of vIRF-1 from the oncogenic KSHV reveals a conserved fold for DNA binding and reinforces its role as a transcription factor.,Hew K, Dahlroth SL, Venkatachalam R, Nasertorabi F, Lim BT, Cornvik T, Nordlund P Nucleic Acids Res. 2013 Feb 21. PMID:23435230[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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