View source for 7sks


==Crystal structure of measles virus matrix protein==
<StructureSection load='7sks' size='340' side='right'caption='[[7sks]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7sks]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Measles_virus_strain_Ichinose-B95a Measles virus strain Ichinose-B95a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SKS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SKS 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]] 2.541&#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=7sks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sks OCA], [https://pdbe.org/7sks PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sks RCSB], [https://www.ebi.ac.uk/pdbsum/7sks PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sks ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MATRX_MEASC MATRX_MEASC] The M protein has a crucial role in virus assembly and interacts with the RNP complex as well as with the viral membrane.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Measles virus, Nipah virus, and multiple other paramyxoviruses cause disease outbreaks in humans and animals worldwide. The paramyxovirus matrix (M) protein mediates virion assembly and budding from host cell membranes. M is thus a key target for antivirals, but few high-resolution structures of paramyxovirus M are available, and we lack the clear understanding of how viral M proteins interact with membrane lipids to mediate viral assembly and egress that is needed to guide antiviral design. Here, we reveal that M proteins associate with phosphatidylserine and phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] at the plasma membrane. Using x-ray crystallography, electron microscopy, and molecular dynamics, we demonstrate that PI(4,5)P2 binding induces conformational and electrostatic changes in the M protein surface that trigger membrane deformation, matrix layer polymerization, and virion assembly.

Measles and Nipah virus assembly: Specific lipid binding drives matrix polymerization.,Norris MJ, Husby ML, Kiosses WB, Yin J, Saxena R, Rennick LJ, Heiner A, Harkins SS, Pokhrel R, Schendel SL, Hastie KM, Landeras-Bueno S, Salie ZL, Lee B, Chapagain PP, Maisner A, Duprex WP, Stahelin RV, Saphire EO Sci Adv. 2022 Jul 22;8(29):eabn1440. doi: 10.1126/sciadv.abn1440. Epub 2022 Jul, 20. PMID:35857835<ref>PMID:35857835</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7sks" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Measles virus strain Ichinose-B95a]]
[[Category: Norris MJ]]
[[Category: Saphire EO]]