View source for 4rlz


==Crystal structure of Norovirus OIF P domain==
<StructureSection load='4rlz' size='340' side='right'caption='[[4rlz]], [[Resolution|resolution]] 1.19&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4rlz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Norovirus_NLV/IF1998/2003/Iraq Norovirus NLV/IF1998/2003/Iraq]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RLZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RLZ 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]] 1.19&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=4rlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rlz OCA], [https://pdbe.org/4rlz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rlz RCSB], [https://www.ebi.ac.uk/pdbsum/4rlz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rlz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6B7R3_9CALI Q6B7R3_9CALI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Norovirus (NoV) causes epidemic acute gastroenteritis in humans, whereby histo-blood group antigens (HBGAs) play an important role in host susceptibility. Each of the two major genogroups (GI and GII) of human NoVs recognizes a unique set of HBGAs through a distinct binding interface that is conserved within a genogroup, indicating a distinct evolutionary path for each genogroup. Here, we characterize a Lewis a (Lea) antigen binding strain (OIF virus) in the GII.21 genotype that does not share the conserved GII binding interface, revealing a new evolution lineage with a distinct HBGA binding interface. Sequence alignment showed that the major residues contributing to the new HBGA binding interface are conserved among most members of the GII.21, as well as a closely related GII.13 genotype. In addition, we found that glycerol inhibits OIF binding to HBGAs, potentially allowing production of cheap antivirals against human NoVs. Taken together, our results reveal a new evolutionary lineage of NoVs selected by HBGAs, a finding that is important for understanding the diversity and widespread nature of NoVs.

A Unique Human Norovirus Lineage with a Distinct HBGA Binding Interface.,Liu W, Chen Y, Jiang X, Xia M, Yang Y, Tan M, Li X, Rao Z PLoS Pathog. 2015 Jul 6;11(7):e1005025. doi: 10.1371/journal.ppat.1005025., eCollection 2015 Jul. PMID:26147716<ref>PMID:26147716</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4rlz" 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 NLV/IF1998/2003/Iraq]]
[[Category: Chen Y]]
[[Category: Jiang X]]
[[Category: Li X]]
[[Category: Liu W]]
[[Category: Rao Z]]
[[Category: Tan M]]
[[Category: Xia M]]