View source for 4ash


==Crystal structure of the NS6 protease from murine norovirus 1==
<StructureSection load='4ash' size='340' side='right'caption='[[4ash]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ash]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Murine_norovirus_1 Murine norovirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ASH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ASH FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Calicivirin Calicivirin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.66 3.4.22.66] </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=4ash FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ash OCA], [https://pdbe.org/4ash PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ash RCSB], [https://www.ebi.ac.uk/pdbsum/4ash PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ash ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Murine noroviruses have emerged as a valuable tool for investigating the molecular basis of infection and pathogenesis of the closely related human noroviruses, which are the major cause of non-bacterial gastroenteritis. The replication of noroviruses relies on the proteolytic processing of a large polyprotein precursor into six non-structural proteins (NS1-2, NS3, NS4, NS5, NS6(pro), NS7(pol)) by the virally-encoded NS6 protease. We report here the crystal structure of MNV NS6(pro), which has been determined to a resolution of 1.6 A. Adventitiously, the crystal contacts are mediated in part by the binding of the C-terminus of NS6(pro) within the peptide-binding cleft of a neighbouring molecule. This insertion occurs for both molecules in the asymmetric unit of the crystal in a manner that is consistent with physiologically-relevant binding, thereby providing two independent views of a protease-peptide complex. Since the NS6(pro) C-terminus is formed in vivo by NS6(pro) processing, these crystal contacts replicate the protease-product complex that is formed immediately following cleavage of the peptide bond at the NS6-NS7 junction. The observed mode of binding of the C-terminal product peptide yields new insights into the structural basis of NS6(pro) specificity.

Structure of a Murine Norovirus NS6 Protease-Product Complex Revealed by Adventitious Crystallisation.,Leen EN, Baeza G, Curry S PLoS One. 2012;7(6):e38723. Epub 2012 Jun 7. PMID:22685603<ref>PMID:22685603</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ash" style="background-color:#fffaf0;"></div>

==See Also==
*[[Virus protease 3D structures|Virus protease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Calicivirin]]
[[Category: Large Structures]]
[[Category: Murine norovirus 1]]
[[Category: Baeza, G]]
[[Category: Curry, S]]
[[Category: Leen, E N]]
[[Category: Calicivirus]]
[[Category: Hydrolase]]
[[Category: Trypsin-like]]