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==Solution NMR structure of the oligomerization domain of respiratory syncytial virus phosphoprotein==
==Solution NMR structure of the oligomerization domain of respiratory syncytial virus phosphoprotein==
<StructureSection load='6yp5' size='340' side='right'caption='[[6yp5]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='6yp5' size='340' side='right'caption='[[6yp5]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6yp5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Respiratory_syncytial_virus Respiratory syncytial virus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YP5 FirstGlance]. <br>
<table><tr><td colspan='2'>Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YP5 FirstGlance]. <br>
</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=6yp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yp5 OCA], [https://pdbe.org/6yp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yp5 RCSB], [https://www.ebi.ac.uk/pdbsum/6yp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yp5 ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=6yp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yp5 OCA], [https://pdbe.org/6yp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yp5 RCSB], [https://www.ebi.ac.uk/pdbsum/6yp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yp5 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The phosphoprotein P of Mononegavirales (MNV) is an essential co-factor of the viral RNA polymerase L. Its prime function is to recruit L to the ribonucleocapsid composed of the viral genome encapsidated by the nucleoprotein N. MNV phosphoproteins often contain a high degree of disorder. In Pneumoviridae phosphoproteins, the only domain with well-defined structure is a small oligomerization domain (POD). We previously characterized the differential disorder in respiratory syncytial virus (RSV) phosphoprotein by NMR. We showed that outside of RSV POD, the intrinsically disordered N-and C-terminal regions displayed a structural and dynamic diversity ranging from random coil to high helical propensity. Here we provide additional insight into the dynamic behavior of PCalpha, a domain that is C-terminal to POD and constitutes the RSV L-binding region together with POD. By using small phosphoprotein fragments centered on or adjacent to POD, we obtained a structural picture of the POD-PCalpha region in solution, at the single residue level by NMR and at lower resolution by complementary biophysical methods. We probed POD-PCalpha inter-domain contacts and showed that small molecules were able to modify the dynamics of PCalpha. These structural properties are fundamental to the peculiar binding mode of RSV phosphoprotein to L, where each of the four protomers binds to L in a different way.
A Structural and Dynamic Analysis of the Partially Disordered Polymerase-Binding Domain in RSV Phosphoprotein.,Cardone C, Caseau CM, Bardiaux B, Thureaux A, Galloux M, Bajorek M, Eleouet JF, Litaudon M, Bontems F, Sizun C Biomolecules. 2021 Aug 17;11(8). pii: biom11081225. doi: 10.3390/biom11081225. PMID:34439894<ref>PMID:34439894</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6yp5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Respiratory syncytial virus]]
[[Category: Bardiaux B]]
[[Category: Bardiaux, B]]
[[Category: Bontems F]]
[[Category: Bontems, F]]
[[Category: Cardone C]]
[[Category: Cardone, C]]
[[Category: Sizun C]]
[[Category: Sizun, C]]
[[Category: Coiled-coil]]
[[Category: Phosphoprotein]]
[[Category: Rna dependent rna polymerase cofactor]]
[[Category: Tetramer]]
[[Category: Viral protein]]

Latest revision as of 09:10, 19 June 2024

Solution NMR structure of the oligomerization domain of respiratory syncytial virus phosphoproteinSolution NMR structure of the oligomerization domain of respiratory syncytial virus phosphoprotein

Structural highlights

Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT
Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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