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==Functional and Structural Characterization of Norovirus GII.6 in Recognizing Histo-blood Group Antigens==
<StructureSection load='7yqg' size='340' side='right'caption='[[7yqg]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7yqg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Norovirus_GII Norovirus GII]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YQG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.698&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=7yqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yqg OCA], [https://pdbe.org/7yqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yqg RCSB], [https://www.ebi.ac.uk/pdbsum/7yqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yqg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A2U9GLY1_9CALI A0A2U9GLY1_9CALI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Noroviruses (NoVs) are the primary cause of acute gastroenteritis worldwide. Histo-blood group antigens (HBGAs) are receptors or attachment factors that affect the prevalence and host susceptibility of NoVs. GII.6 NoV is one of the predominant genotypes in humans, which recognizes the type ABO secretor of HBGAs. However, the structural basis of GII.6 NoV's interaction with HBGAs receptors remains elusive. In this study, we investigated the binding features of the GII.6 strain to HBGAs using saliva- and glycan-ELISA assays and characterized the molecular basis of the GII.6 virus that recognizes H disaccharide. We showed that the GII.6 âP domain recognized some A and O secretor's saliva samples, most B secretor's saliva samples, and H disaccharide antigen, but did not bind non-secretors' saliva. Further, we determined the crystal structures of GII.6 and its complex with H disaccharides at 1.7 âA, revealing that the P domain of GII.6 shares the conventional binding interface and mode of GII HBGAs. Single residue mutations at the GII.6-H binding sites could inhibit the binding of GII.6 to HBGAs, demonstrating that the interaction residues were crucial in maintaining NoV-glycan integrity. Finally, structural and sequence analyses showed that the major residues of the GII.6-H interaction were conserved among NoVs in the GII genogroup. Taken together, our study characterized the functional and structural features of GII.6 that allow it to interact with HBGAs, and shed light on NoV evolution, epidemiology, and anti-viral drug development.

Functional and structural characterization of Norovirus GII.6 in recognizing histo-blood group antigens.,Cong X, Li HB, Sun XM, Qi JX, Zhang Q, Duan ZJ, Xu Y, Liu WL Virol Sin. 2023 Feb;38(1):56-65. doi: 10.1016/j.virs.2022.09.010. Epub 2022 Oct , 7. PMID:36216242<ref>PMID:36216242</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7yqg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Norovirus GII]]
[[Category: Cong X]]
[[Category: Duan ZJ]]