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==1.15 A resolution structure of Norovirus 3CL protease in complex with a triazole-based macrocyclic inhibitor== | |||
<StructureSection load='6bid' size='340' side='right' caption='[[6bid]], [[Resolution|resolution]] 1.15Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6bid]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BID OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BID FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DW4:benzyl+[(8S,11S,14S)-11-(cyclohexylmethyl)-8-(hydroxymethyl)-5,10,13-trioxo-1,4,9,12,17,18-hexaazabicyclo[14.2.1]nonadeca-16(19),17-dien-14-yl]carbamate'>DW4</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calicivirin Calicivirin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.66 3.4.22.66] </span></td></tr> | |||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6bid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bid OCA], [http://pdbe.org/6bid PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bid RCSB], [http://www.ebi.ac.uk/pdbsum/6bid PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bid ProSAT]</span></td></tr> | ||
[[Category: Battaile, K | </table> | ||
[[Category: | == Function == | ||
[[Category: | [[http://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> | ||
[[Category: Kankanamalage, A | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Calicivirin]] | |||
[[Category: Battaile, K P]] | |||
[[Category: Chang, K O]] | |||
[[Category: Groutas, W C]] | |||
[[Category: Kankanamalage, A C.G]] | |||
[[Category: Kim, Y]] | [[Category: Kim, Y]] | ||
[[Category: Lovell, S]] | [[Category: Lovell, S]] | ||
[[Category: Rathnayake, A | [[Category: Mehzabeen, N]] | ||
[[Category: Rathnayake, A D]] | |||
[[Category: Weerawarna, P M]] | |||
[[Category: Antiviral inhibitor]] | |||
[[Category: Hydrolase-hydrolase inhibitor complex]] | |||
[[Category: Norovirus]] | |||
[[Category: Norwalk virus]] | |||
[[Category: Protease]] | |||
[[Category: Triazole-based macrocyclic inhibitor]] | |||
Revision as of 15:12, 7 November 2018
1.15 A resolution structure of Norovirus 3CL protease in complex with a triazole-based macrocyclic inhibitor1.15 A resolution structure of Norovirus 3CL protease in complex with a triazole-based macrocyclic inhibitor
Structural highlights
Function[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.[1] [2] NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity.[3] [4] Protein P22 may play a role in targeting replication complex to intracellular membranes.[5] [6] 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.[7] [8] 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).[9] [10] 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).[11] [12] References
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