View source for 9ccv


==Crystal structure of human respiratory syncytial virus NS1 bound to human MED25 ACID==
<StructureSection load='9ccv' size='340' side='right'caption='[[9ccv]], [[Resolution|resolution]] 2.53&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9ccv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_respiratory_syncytial_virus_A Human respiratory syncytial virus A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9CCV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9CCV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.53&#8491;</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=9ccv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ccv OCA], [https://pdbe.org/9ccv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ccv RCSB], [https://www.ebi.ac.uk/pdbsum/9ccv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ccv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E0WLW8_HRSV E0WLW8_HRSV] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Mediator complex facilitates interactions between transcription factors and RNA polymerase II, a process that is required for host gene transcription, including in response to viral infections. Among the many subunits in the Mediator complex, the MED25 subunit has been shown to be a target for viral activators during infection. Here we provide the molecular basis for the interaction between human respiratory syncytial virus (hRSV) nonstructural 1 protein (NS1) and the activator interaction domain (ACID) of MED25. The X-ray crystal structure of the complex revealed that NS1 straddles and binds two faces of MED25 ACID. This interaction is distinct from previously known viral activators. Importantly, our data support the conformational flexibility of viral transcriptional regulators. Furthermore, ChIP-seq and RNA-seq analysis identified the ATF3 transcription factor and a role for NS1/Mediator/ATF3 interaction in host gene regulation in hRSV infections. Our findings provide a molecular basis for hRSV NS1-based regulation of host gene transcription and reveal how viruses exploit the conformational heterogeneity at fuzzy transcription activator interfaces.

Molecular basis for human respiratory syncytial virus transcriptional regulator NS1 interactions with MED25.,Kalita P, Khatavkar O, Uwase G, Korshunova Y, Hu Y, Wagner ND, Xu J, Pan J, Nix JC, Gross ML, Brody SL, Borek D, Amarasinghe GK, Payton JE, Leung DW Nat Commun. 2025 Mar 25;16(1):2883. doi: 10.1038/s41467-025-58216-4. PMID:40128225<ref>PMID:40128225</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9ccv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Human respiratory syncytial virus A]]
[[Category: Large Structures]]
[[Category: Amarasinghe GK]]
[[Category: Borek DM]]
[[Category: Kalita P]]
[[Category: Leung DW]]