4uft: Difference between revisions
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<StructureSection load='4uft' size='340' side='right' caption='[[4uft]], [[Resolution|resolution]] 4.30Å' scene=''> | <StructureSection load='4uft' size='340' side='right' caption='[[4uft]], [[Resolution|resolution]] 4.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4uft]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Spodoptera_frugiperda Spodoptera frugiperda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UFT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UFT FirstGlance]. <br> | <table><tr><td colspan='2'>[[4uft]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Meash Meash] and [http://en.wikipedia.org/wiki/Spodoptera_frugiperda Spodoptera frugiperda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UFT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UFT FirstGlance]. <br> | ||
</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=4uft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uft OCA], [http://pdbe.org/4uft PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uft RCSB], [http://www.ebi.ac.uk/pdbsum/4uft PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uft ProSAT]</span></td></tr> | </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=4uft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uft OCA], [http://pdbe.org/4uft PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uft RCSB], [http://www.ebi.ac.uk/pdbsum/4uft PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uft ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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</div> | </div> | ||
<div class="pdbe-citations 4uft" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4uft" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Meash]] | |||
[[Category: Spodoptera frugiperda]] | [[Category: Spodoptera frugiperda]] | ||
[[Category: Desfosses, A]] | [[Category: Desfosses, A]] | ||
Revision as of 06:00, 16 November 2017
Structure of the helical Measles virus nucleocapsidStructure of the helical Measles virus nucleocapsid
Structural highlights
Function[NCAP_MEASH] Encapsidates the genome in a ratio of 1 N per 6 ribonucleotides, protecting it from nucleases. The nucleocapsid (NC) has a helical structure with either 12.35 or 11.64 N per turn, approximately 20 nm in diameter, with a hollow central cavity approximately 5 nm in diameter. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. During replication, encapsidation by N is coupled to RNA synthesis and all replicative products are resistant to nucleases. N is released in the blood following lysis of measles infected cells, it interacts then with human FCGR2B on immune cells, inducing apoptosis and blocking inflammatory immune response. Ntail binds to a protein on human thymic epithelial cells, termed Nucleoprotein Receptor (NR), inducing growth arrest. Publication Abstract from PubMedMeasles is a highly contagious human disease. We used cryo-electron microscopy and single particle-based helical image analysis to determine the 4.3 A resolution structure of the helical nucleocapsid formed by the folded domain of the Measles Virus nucleoprotein encapsidating an RNA. The resulting pseudoatomic model of the Measles Virus nucleocapsid offers important insights into the mechanism of the helical polymerisation of nucleocapsids of negative-strand RNA viruses, in particular via the exchange subdomains of the nucleoprotein.The structure reveals the mode of the nucleoprotein-RNA interaction and explains why each nucleoprotein of Measles Virus binds six nucleotides whereas the Respiratory Syncytial Virus nucleoprotein binds seven. It provides a rational basis for further analysis of Measles Virus replication and transcription, and reveals potential targets for drug design. Near-atomic cryo-EM structure of the helical measles virus nucleocapsid.,Gutsche I, Desfosses A, Effantin G, Ling WL, Haupt M, Ruigrok RW, Sachse C, Schoehn G Science. 2015 Apr 16. pii: aaa5137. PMID:25883315[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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