2lnc

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{{STRUCTURE_2lnc| PDB=2lnc | SCENE= }}
 
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===Solution NMR structure of Norwalk virus protease===
 
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{{ABSTRACT_PUBMED_23319456}}
 
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==Function==
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==Solution NMR structure of Norwalk virus protease==
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[[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>
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<StructureSection load='2lnc' size='340' side='right'caption='[[2lnc]]' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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</table>
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== Function ==
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[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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==About this Structure==
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==See Also==
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[[2lnc]] is a 1 chain structure with sequence from [http://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].
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*[[Virus protease 3D structures|Virus protease 3D structures]]
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== References ==
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==Reference==
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<references/>
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<references group="xtra"/><references/>
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__TOC__
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[[Category: Calicivirin]]
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</StructureSection>
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[[Category: Norovirus hu/1968/us]]
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[[Category: Large Structures]]
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[[Category: Anbanandam, A.]]
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[[Category: Norovirus Hu/1968/US]]
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[[Category: Chang, K.]]
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[[Category: Anbanandam A]]
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[[Category: Hiromasa, Y.]]
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[[Category: Chang K]]
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[[Category: Kim, Y.]]
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[[Category: Hiromasa Y]]
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[[Category: Prakash, O.]]
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[[Category: Kim Y]]
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[[Category: Takahashi, D.]]
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[[Category: Prakash O]]
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[[Category: Calicivirus]]
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[[Category: Takahashi D]]
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[[Category: Chymotrypsin-like protease]]
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[[Category: Hydrolase]]
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[[Category: Viral protease]]
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Current revision

Solution NMR structure of Norwalk virus protease

PDB ID 2lnc

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