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4opo

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<StructureSection load='4opo' size='340' side='right'caption='[[4opo]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='4opo' size='340' side='right'caption='[[4opo]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4opo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Norovirus_hu/gii-4/kumamoto5/2006/jp Norovirus hu/gii-4/kumamoto5/2006/jp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OPO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OPO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4opo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Norovirus_Hu/GII-4/Kumamoto5/2006/JP Norovirus Hu/GII-4/Kumamoto5/2006/JP]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OPO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OPO FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oox|4oox]], [[4op7|4op7]], [[4oos|4oos]], [[4oov|4oov]], [[4ops|4ops]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900123:Lewis+B+antigen,+beta+anomer'>PRD_900123</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AB447457 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=546987 Norovirus Hu/GII-4/Kumamoto5/2006/JP])</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=4opo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4opo OCA], [https://pdbe.org/4opo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4opo RCSB], [https://www.ebi.ac.uk/pdbsum/4opo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4opo ProSAT]</span></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=4opo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4opo OCA], [http://pdbe.org/4opo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4opo RCSB], [http://www.ebi.ac.uk/pdbsum/4opo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4opo ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/B5BTT5_9CALI B5BTT5_9CALI]
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Human noroviruses are the dominant cause of outbreaks of gastroenteritis around the world. Human norovirus interacts with the polymorphic human histo-blood group antigens (HBGAs) and this interaction is thought to be important for infection. Indeed, synthetic HBGAs or HBGA-expressing enteric bacteria were shown to enhance norovirus infection in B cells. A number of studies have found a possible relationship between HBGA type and norovirus susceptibility. The genogroup II genotype 4 (GII.4) noroviruses are the dominant cluster, evolve every other year, and are thought to modify their binding interactions to different HBGA types. Here, we show the high-resolution X-ray crystal structures of the capsid protruding (P) domains from epidemic GII.4 variants in 2004, 2006, and 2012, co-crystallized with a panel of HBGA types (H type 2, Lewis Y, Lewis B, Lewis A, Lewis X, A-type, and B-type). Many of the HBGA binding interactions were found to be complex, involving capsid loop movements, alternative HBGA conformations, and HBGA rotations. We showed that a loop (residues 391-395) was elegantly repositioned in order to allow for Lewis Y binding. This loop was also slightly shifted to provide direct hydrogen and water-mediated bonds with Lewis B. We considered that the flexible loop modulated Lewis HBGA binding. The GII.4 noroviruses have dominated outbreaks over the past decade, which may be explained by their exquisite HBGA binding mechanisms, their fondness for Lewis HBGAs, and their temporal amino acid modifications. IMPORTANCE: Our data provides a comprehensive picture of GII.4 P domain and HBGA binding interactions. The exceptionally high resolutions of our X-ray crystal structures allowed us to accurately recognize novel GII.4 P domain interactions with numerous HBGA types. We showed that the GII.4 P domain HBGA interactions involved complex binding mechanisms that were not previously observed in norovirus structural studies. Many of the GII.4 P domain HBGA interactions we identified were negative in earlier ELISA-based studies. Altogether, we showed that the GII.4 norovirus P domains could accommodate numerous HBGA types.
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Human Noroviruses' Fondness of Histo-Blood Group Antigens.,Singh BK, Leuthold MM, Hansman GS J Virol. 2014 Nov 26. pii: JVI.02968-14. PMID:25428879<ref>PMID:25428879</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 4opo" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Norovirus hu/gii-4/kumamoto5/2006/jp]]
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[[Category: Norovirus Hu/GII-4/Kumamoto5/2006/JP]]
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[[Category: Hansman, G S]]
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[[Category: Hansman GS]]
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[[Category: Singh, B K]]
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[[Category: Singh BK]]
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[[Category: Norovirus]]
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[[Category: Protruding domain]]
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[[Category: Viral capsid protein]]
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[[Category: Viral protein]]
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Current revision

Crystal structure of P domain from norovirus strain Saga4 in complex with HBGA type Leb (tetraglycan)

PDB ID 4opo

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