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| | ==Crystal Structure of Murine Norovirus Protruding (P) Domain== | | ==Crystal Structure of Murine Norovirus Protruding (P) Domain== |
| - | <StructureSection load='3lq6' size='340' side='right' caption='[[3lq6]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3lq6' size='340' side='right'caption='[[3lq6]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3lq6]] is a 2 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=3LQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LQ6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3lq6]] 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=3LQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LQ6 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lqe|3lqe]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <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=3lq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lq6 OCA], [http://pdbe.org/3lq6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lq6 RCSB], [http://www.ebi.ac.uk/pdbsum/3lq6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lq6 ProSAT]</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=3lq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lq6 OCA], [https://pdbe.org/3lq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lq6 RCSB], [https://www.ebi.ac.uk/pdbsum/3lq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lq6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q2V8W4_9CALI Q2V8W4_9CALI] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Virus coat protein|Virus coat protein]] | + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Murine norovirus 1]] | | [[Category: Murine norovirus 1]] |
| - | [[Category: Rubin, J R]] | + | [[Category: Rubin JR]] |
| - | [[Category: Stuckey, J A]] | + | [[Category: Stuckey JA]] |
| - | [[Category: Viral capsid protein]]
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| - | [[Category: Viral protein]]
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| Structural highlights
Function
Q2V8W4_9CALI
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Murine noroviruses (MNV) are closely related to the human noroviruses (HuNoV), which cause the majority of nonbacterial gastroenteritis. Unlike HuNoV, MNV grow in culture and in a small-animal model that represents a tractable model to study norovirus biology. To begin a detailed investigation of molecular events that occur during norovirus binding to cells, the crystallographic structure of the murine norovirus 1 (MNV-1) capsid protein protruding (P) domain has been determined. Crystallization of the bacterially expressed protein yielded two different crystal forms (Protein Data Bank identifiers [PDB ID], 3LQ6 and 3LQE). Comparison of the structures indicated a large degree of structural mobility in loops on the surface of the P2 subdomain. Specifically, the A'-B' and E'-F' loops were found in open and closed conformations. These regions of high mobility include the known escape mutation site for the neutralizing antibody A6.2 and an attenuation mutation site, which arose after serial passaging in culture and led to a loss in lethality in STAT1(-/-) mice, respectively. Modeling of a Fab fragment and crystal structures of the P dimer into the cryoelectron microscopy three-dimensional (3D) image reconstruction of the A6.2/MNV-1 complex indicated that the closed conformation is most likely bound to the Fab fragment and that the antibody contact is localized to the A'-B' and E'-F' loops. Therefore, we hypothesize that these loop regions and the flexibility of the P domains play important roles during MNV-1 binding to the cell surface.
High-resolution x-ray structure and functional analysis of the murine norovirus 1 capsid protein protruding domain.,Taube S, Rubin JR, Katpally U, Smith TJ, Kendall A, Stuckey JA, Wobus CE J Virol. 2010 Jun;84(11):5695-705. Epub 2010 Mar 24. PMID:20335262[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Taube S, Rubin JR, Katpally U, Smith TJ, Kendall A, Stuckey JA, Wobus CE. High-resolution x-ray structure and functional analysis of the murine norovirus 1 capsid protein protruding domain. J Virol. 2010 Jun;84(11):5695-705. Epub 2010 Mar 24. PMID:20335262 doi:10.1128/JVI.00316-10
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