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==Crystal structure of the Nipah virus RNA free nucleoprotein- phosphoprotein complex==
==Crystal structure of the Nipah virus RNA free nucleoprotein- phosphoprotein complex==
<StructureSection load='4co6' size='340' side='right' caption='[[4co6]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='4co6' size='340' side='right'caption='[[4co6]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4co6]] is a 6 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CO6 FirstGlance]. <br>
<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><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene><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]] 2.498&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4co6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4co6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4co6 RCSB], [http://www.ebi.ac.uk/pdbsum/4co6 PDBsum]</span></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>
</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&reg;/PubMed&reg;, 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__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Blackledge, M.]]
[[Category: Henipavirus nipahense]]
[[Category: Bourhis, J M.]]
[[Category: Large Structures]]
[[Category: Jamin, M.]]
[[Category: Blackledge M]]
[[Category: Jensen, M R.]]
[[Category: Bourhis JM]]
[[Category: Lawrence, P.]]
[[Category: Jamin M]]
[[Category: Ruigrok, R W.H.]]
[[Category: Jensen MR]]
[[Category: Tarbouriech, N.]]
[[Category: Lawrence P]]
[[Category: Volchkov, V.]]
[[Category: Ruigrok RWH]]
[[Category: Yabukarksi, F.]]
[[Category: Tarbouriech N]]
[[Category: Chaperone]]
[[Category: Volchkov V]]
[[Category: Paramyxovirus]]
[[Category: Yabukarksi F]]
[[Category: Viral protein]]
[[Category: Viral replication]]

Latest revision as of 08:24, 23 October 2024

Crystal structure of the Nipah virus RNA free nucleoprotein- phosphoprotein complex

4co6, resolution 2.50Å

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