View source for 5lkg


==Protruding domain of GII.17 norovirus Kawasaki308 in complex with 2-fucosyllactose (2'FL)==
<StructureSection load='5lkg' size='340' side='right'caption='[[5lkg]], [[Resolution|resolution]] 1.51&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lkg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Norovirus_Hu/GII/JP/2015/GII.P17_GII.17/Kawasaki308 Norovirus Hu/GII/JP/2015/GII.P17_GII.17/Kawasaki308]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LKG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LKG 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]] 1.51&#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=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5lkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lkg OCA], [https://pdbe.org/5lkg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lkg RCSB], [https://www.ebi.ac.uk/pdbsum/5lkg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lkg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0E4B1P1_9CALI A0A0E4B1P1_9CALI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human noroviruses are the leading cause of outbreaks of acute gastroenteritis. Norovirus interactions with histo-blood group antigens (HBGAs) are known to be important for an infection. In this study, we identified the HBGA binding pocket for an emerging GII genotype 17 (GII.17) variant using X-ray crystallography. The GII.17 variant bound the HBGA with an equivalent set of residues as the leading pandemic GII.4 variants. These structural data highlights the conserved nature of HBGA binding site between prevalent GII noroviruses. Noroviruses also interact with human milk oligosaccharides (HMOs), which mimic HBGAs and may function as receptor decoys. We previously showed that HMOs inhibited the binding of rarely detected GII.10 norovirus to HBGAs. We now found that an HMO, 2'-fucosyllactose (2'FL), additionally blocked both the GI.1 and GII.17 noroviruses from binding to HBGAs. Together, these findings provide evidence that 2'FL might function as a broadly reactive antiviral against multiple norovirus genogroups.

Human norovirus inhibition by a human milk oligosaccharide.,Koromyslova A, Tripathi S, Morozov V, Schroten H, Hansman GS Virology. 2017 May 12;508:81-89. doi: 10.1016/j.virol.2017.04.032. PMID:28505592<ref>PMID:28505592</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5lkg" style="background-color:#fffaf0;"></div>

==See Also==
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Norovirus Hu/GII/JP/2015/GII P17_GII 17/Kawasaki308]]
[[Category: Hansman GS]]
[[Category: Morozov V]]
[[Category: Singh BK]]