6htl
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HTL FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6htl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6htl OCA], [http://pdbe.org/6htl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6htl RCSB], [http://www.ebi.ac.uk/pdbsum/6htl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6htl ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <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: Longhi, S]] | ||
| + | [[Category: Schramm, A]] | ||
| + | [[Category: 3-10 helix]] | ||
| + | [[Category: Alpha helix]] | ||
| + | [[Category: Coiled-coil]] | ||
| + | [[Category: Tetramer]] | ||
| + | [[Category: Viral protein]] | ||
Revision as of 22:45, 5 June 2019
Measles Phosphoprotein Coiled-Coil Domain IPKI Variant
| |||||||||||
