6crj

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==Mouse norovirus model using the crystal structure of MNV P domain and the Norwalkvirus shell domain==
==Mouse norovirus model using the crystal structure of MNV P domain and the Norwalkvirus shell domain==
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<StructureSection load='6crj' size='340' side='right' caption='[[6crj]], [[Resolution|resolution]] 8.00&Aring;' scene=''>
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<SX load='6crj' size='340' side='right' viewer='molstar' caption='[[6crj]], [[Resolution|resolution]] 8.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6crj]] is a 3 chain structure with sequence from [http://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=6CRJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CRJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6crj]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Murine_norovirus_1 Murine norovirus 1] and [https://en.wikipedia.org/wiki/Norwalk_virus Norwalk virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CRJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CRJ FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ORF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=223997 Murine norovirus 1])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8&#8491;</td></tr>
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<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=6crj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6crj OCA], [http://pdbe.org/6crj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6crj RCSB], [http://www.ebi.ac.uk/pdbsum/6crj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6crj ProSAT]</span></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=6crj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6crj OCA], [https://pdbe.org/6crj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6crj RCSB], [https://www.ebi.ac.uk/pdbsum/6crj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6crj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CAPSD_NVN68 CAPSD_NVN68]] Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells by binding histo-blood group antigens present on gastroduodenal epithelial cells.<ref>PMID:16840313</ref> Soluble capsid protein may play a role in viral immunoevasion.<ref>PMID:16840313</ref>
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[https://www.uniprot.org/uniprot/Q2V8W4_9CALI Q2V8W4_9CALI] [https://www.uniprot.org/uniprot/CAPSD_NVN68 CAPSD_NVN68] Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells by binding histo-blood group antigens present on gastroduodenal epithelial cells.<ref>PMID:16840313</ref> Soluble capsid protein may play a role in viral immunoevasion.<ref>PMID:16840313</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Our previous structural studies on intact, infectious murine norovirus 1 (MNV-1) virions demonstrated that the receptor binding protruding (P) domains are lifted off the inner shell of the virus. Here, the three-dimensional (3D) reconstructions of recombinant rabbit hemorrhagic disease virus (rRHDV) virus-like particles (VLPs) and intact MNV-1 were determined to approximately 8-A resolution. rRHDV also has a raised P domain, and therefore, this conformation is independent of infectivity and genus. The atomic structure of the MNV-1 P domain was used to interpret the MNV-1 reconstruction. Connections between the P and shell domains and between the floating P domains were modeled. This observed P-domain flexibility likely facilitates virus-host receptor interactions.
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High-resolution cryo-electron microscopy structures of murine norovirus 1 and rabbit hemorrhagic disease virus reveal marked flexibility in the receptor binding domains.,Katpally U, Voss NR, Cavazza T, Taube S, Rubin JR, Young VL, Stuckey J, Ward VK, Virgin HW 4th, Wobus CE, Smith TJ J Virol. 2010 Jun;84(11):5836-41. doi: 10.1128/JVI.00314-10. Epub 2010 Mar 24. PMID:20335264<ref>PMID:20335264</ref>
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==See Also==
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6crj" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Large Structures]]
[[Category: Murine norovirus 1]]
[[Category: Murine norovirus 1]]
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[[Category: Smith, T J]]
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[[Category: Norwalk virus]]
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[[Category: Mouse]]
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[[Category: Smith TJ]]
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[[Category: Norovirus]]
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[[Category: Virus]]
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Current revision

Mouse norovirus model using the crystal structure of MNV P domain and the Norwalkvirus shell domain

6crj, resolution 8.00Å

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