4rm0: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='4rm0' size='340' side='right'caption='[[4rm0]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='4rm0' size='340' side='right'caption='[[4rm0]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4rm0]] is a 2 chain structure with sequence from [http://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=4RM0 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[4rm0]] is a 2 chain structure with sequence from [http://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=4RM0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4RM0 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr> | </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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rlz|4rlz]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rlz|4rlz]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=4rm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rm0 OCA], [http://pdbe.org/4rm0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rm0 RCSB], [http://www.ebi.ac.uk/pdbsum/4rm0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rm0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 08:38, 5 August 2020
Crystal structure of Norovirus OIF P domain in complex with Lewis a trisaccharideCrystal structure of Norovirus OIF P domain in complex with Lewis a trisaccharide
Structural highlights
Publication Abstract from PubMedNorovirus (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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||