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==Solution NMR structure of Norwalk virus protease==
==Solution NMR structure of Norwalk virus protease==
<StructureSection load='2lnc' size='340' side='right'caption='[[2lnc]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2lnc' size='340' side='right'caption='[[2lnc]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2lnc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hu/nv/nv/1968/us Hu/nv/nv/1968/us]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LNC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LNC FirstGlance]. <br>
<table><tr><td colspan='2'>[[2lnc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Norovirus_Hu/1968/US Norovirus Hu/1968/US]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LNC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LNC FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ORF1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=524364 Hu/NV/NV/1968/US])</td></tr>
</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=2lnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lnc OCA], [https://pdbe.org/2lnc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lnc RCSB], [https://www.ebi.ac.uk/pdbsum/2lnc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lnc ProSAT]</span></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=2lnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lnc OCA], [https://pdbe.org/2lnc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lnc RCSB], [https://www.ebi.ac.uk/pdbsum/2lnc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lnc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/POLG_NVN68 POLG_NVN68]] Protein p48 may play a role in viral replication by interacting with host VAPA, a vesicle-associated membrane protein that plays a role in SNARE-mediated vesicle fusion. This interaction may target replication complex to intracellular membranes.<ref>PMID:569187</ref> <ref>PMID:11160659</ref>  NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity.<ref>PMID:569187</ref> <ref>PMID:11160659</ref>  Protein P22 may play a role in targeting replication complex to intracellular membranes.<ref>PMID:569187</ref> <ref>PMID:11160659</ref>  Viral genome-linked protein is covalently linked to the 5'-end of the positive-strand, negative-strand genomic RNAs and subgenomic RNA. Acts as a genome-linked replication primer. May recruit ribosome to viral RNA thereby promoting viral proteins translation.<ref>PMID:569187</ref> <ref>PMID:11160659</ref>  3C-like protease processes the polyprotein: 3CLpro-RdRp is first released by autocleavage, then all other proteins are cleaved. May cleave host polyadenylate-binding protein thereby inhibiting cellular translation (By similarity).<ref>PMID:569187</ref> <ref>PMID:11160659</ref>  RNA-directed RNA polymerase replicates genomic and antigenomic RNA by recognizing replications specific signals. Transcribes also a subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This sgRNA encodes for structural proteins. Catalyzes the covalent attachment VPg with viral RNAs (By similarity).<ref>PMID:569187</ref> <ref>PMID:11160659</ref>
[https://www.uniprot.org/uniprot/POLG_NVN68 POLG_NVN68] Protein p48 may play a role in viral replication by interacting with host VAPA, a vesicle-associated membrane protein that plays a role in SNARE-mediated vesicle fusion. This interaction may target replication complex to intracellular membranes.<ref>PMID:569187</ref> <ref>PMID:11160659</ref>  NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity.<ref>PMID:569187</ref> <ref>PMID:11160659</ref>  Protein P22 may play a role in targeting replication complex to intracellular membranes.<ref>PMID:569187</ref> <ref>PMID:11160659</ref>  Viral genome-linked protein is covalently linked to the 5'-end of the positive-strand, negative-strand genomic RNAs and subgenomic RNA. Acts as a genome-linked replication primer. May recruit ribosome to viral RNA thereby promoting viral proteins translation.<ref>PMID:569187</ref> <ref>PMID:11160659</ref>  3C-like protease processes the polyprotein: 3CLpro-RdRp is first released by autocleavage, then all other proteins are cleaved. May cleave host polyadenylate-binding protein thereby inhibiting cellular translation (By similarity).<ref>PMID:569187</ref> <ref>PMID:11160659</ref>  RNA-directed RNA polymerase replicates genomic and antigenomic RNA by recognizing replications specific signals. Transcribes also a subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This sgRNA encodes for structural proteins. Catalyzes the covalent attachment VPg with viral RNAs (By similarity).<ref>PMID:569187</ref> <ref>PMID:11160659</ref>  
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Calicivirin]]
[[Category: Hu/nv/nv/1968/us]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Anbanandam, A]]
[[Category: Norovirus Hu/1968/US]]
[[Category: Chang, K]]
[[Category: Anbanandam A]]
[[Category: Hiromasa, Y]]
[[Category: Chang K]]
[[Category: Kim, Y]]
[[Category: Hiromasa Y]]
[[Category: Prakash, O]]
[[Category: Kim Y]]
[[Category: Takahashi, D]]
[[Category: Prakash O]]
[[Category: Calicivirus]]
[[Category: Takahashi D]]
[[Category: Chymotrypsin-like protease]]
[[Category: Hydrolase]]
[[Category: Viral protease]]