View source for 9ftf


==Crystal structure of the Connecting Domain of the Nipah virus Large protein==
<StructureSection load='9ftf' size='340' side='right'caption='[[9ftf]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9ftf]] is a 1 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=9FTF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FTF 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]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=9ftf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ftf OCA], [https://pdbe.org/9ftf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ftf RCSB], [https://www.ebi.ac.uk/pdbsum/9ftf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ftf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/L_NIPAV L_NIPAV] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nipah virus is a highly virulent zoonotic paramyxovirus causing severe respiratory and neurological disease. Despite its lethality, there is no approved treatment for Nipah virus infection. The viral polymerase complex, composed of the polymerase (L) and phosphoprotein (P), replicates and transcribes the viral RNA genome. Here, we describe structures of the Nipah virus L-P polymerase complex and the L-protein's Connecting Domain (CD). The cryo-electron microscopy L-P complex structure reveals the organization of the RNA-dependent RNA polymerase (RdRp) and polyribonucleotidyl transferase (PRNTase) domains of the L-protein, and shows how the P-protein, which forms a tetramer, interacts with the RdRp-domain of the L-protein. The crystal structure of the CD-domain alone reveals binding of three Mg ions. Modelling of this domain onto an AlphaFold 3 model of an RNA-L-P complex suggests a catalytic role for one Mg ion in mRNA capping. These findings offer insights into the structural details of the L-P polymerase complex and the molecular interactions between L-protein and P-protein, shedding light on the mechanisms of the replication machinery. This work will underpin efforts to develop antiviral drugs that target the polymerase complex of Nipah virus.

Structure of the Nipah virus polymerase complex.,Balikci E, Gunl F, Carrique L, Keown JR, Fodor E, Grimes JM EMBO J. 2024 Dec 30. doi: 10.1038/s44318-024-00321-z. PMID:39739115<ref>PMID:39739115</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9ftf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Henipavirus nipahense]]
[[Category: Large Structures]]
[[Category: Balikci E]]
[[Category: Carrique L]]
[[Category: Fodor E]]
[[Category: Grimes JM]]
[[Category: Gunl F]]
[[Category: Keown JR]]