6htl: Difference between revisions
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The | ==Measles Phosphoprotein Coiled-Coil Domain IPKI Variant== | ||
<StructureSection load='6htl' size='340' side='right'caption='[[6htl]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6htl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Measles_morbillivirus Measles morbillivirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HTL 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]] 2.3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=6htl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6htl OCA], [https://pdbe.org/6htl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6htl RCSB], [https://www.ebi.ac.uk/pdbsum/6htl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6htl ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q83623_9MONO Q83623_9MONO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The polymerase of negative-stranded RNA viruses consists of the large protein (L) and the phosphoprotein (P), the latter serving both as a chaperon and a cofactor for L. We mapped within measles virus (MeV) P the regions responsible for binding and stabilizing L and showed that the coiled-coil multimerization domain (MD) of P is required for gene expression. MeV MD is kinked as a result of the presence of a stammer. Both restoration of the heptad regularity and displacement of the stammer strongly decrease or abrogate activity in a minigenome assay. By contrast, P activity is rather tolerant of substitutions within the stammer. Single substitutions at the "a" or "d" hydrophobic anchor positions with residues of variable hydrophobicity revealed that P functionality requires a narrow range of cohesiveness of its MD. Results collectively indicate that, beyond merely ensuring P oligomerization, the MD finely tunes viral gene expression through its cohesiveness. | |||
Regulation of measles virus gene expression by P protein coiled-coil properties.,Bloyet LM, Schramm A, Lazert C, Raynal B, Hologne M, Walker O, Longhi S, Gerlier D Sci Adv. 2019 May 8;5(5):eaaw3702. doi: 10.1126/sciadv.aaw3702. eCollection 2019 , May. PMID:31086822<ref>PMID:31086822</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6htl" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Measles morbillivirus]] | |||
[[Category: Longhi S]] | |||
[[Category: Schramm A]] | |||
Latest revision as of 11:39, 24 January 2024
Measles Phosphoprotein Coiled-Coil Domain IPKI Variant
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