4co6: Difference between revisions
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The | ==Crystal structure of the Nipah virus RNA free nucleoprotein- phosphoprotein complex== | ||
<StructureSection load='4co6' size='340' side='right'caption='[[4co6]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4co6]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Henipavirus_nipahense Henipavirus nipahense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CO6 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]] 2.498Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4co6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4co6 OCA], [https://pdbe.org/4co6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4co6 RCSB], [https://www.ebi.ac.uk/pdbsum/4co6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4co6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NCAP_NIPAV NCAP_NIPAV] Encapsidates the genome protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Nipah virus (NiV) is a highly pathogenic emergent paramyxovirus causing deadly encephalitis in humans. Its replication requires a constant supply of unassembled nucleoprotein (N0) in complex with its viral chaperone, the phosphoprotein (P). To elucidate the chaperone function of P, we reconstituted NiV the N0-P core complex and determined its crystal structure. The binding of the N-terminal region of P blocks the polymerization of N by interfering with subdomain exchange between N protomers and keeps N0 in an open conformation, ready to grasp an RNA molecule. We found that a peptide derived from the N-binding region of P protects cells against viral infection and demonstrated by structure-based mutagenesis that this peptide acts by inhibiting N0-P formation. These results provide new insights about the assembly of N along genomic RNA and validate the N0-P complex as a target for drug development. | |||
Structure of Nipah virus unassembled nucleoprotein in complex with its viral chaperone.,Yabukarski F, Lawrence P, Tarbouriech N, Bourhis JM, Delaforge E, Jensen MR, Ruigrok RW, Blackledge M, Volchkov V, Jamin M Nat Struct Mol Biol. 2014 Aug 10. doi: 10.1038/nsmb.2868. PMID:25108352<ref>PMID:25108352</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4co6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Henipavirus nipahense]] | |||
[[Category: Large Structures]] | |||
[[Category: Blackledge M]] | |||
[[Category: Bourhis JM]] | |||
[[Category: Jamin M]] | |||
[[Category: Jensen MR]] | |||
[[Category: Lawrence P]] | |||
[[Category: Ruigrok RWH]] | |||
[[Category: Tarbouriech N]] | |||
[[Category: Volchkov V]] | |||
[[Category: Yabukarksi F]] | |||