6k2o
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='6k2o' size='340' side='right'caption='[[6k2o]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='6k2o' size='340' side='right'caption='[[6k2o]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6k2o]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K2O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K2O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6k2o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Group_a_rotaviruses Group a rotaviruses]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K2O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K2O 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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | </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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
<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=6k2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k2o OCA], [http://pdbe.org/6k2o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k2o RCSB], [http://www.ebi.ac.uk/pdbsum/6k2o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k2o ProSAT]</span></td></tr> | <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=6k2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k2o OCA], [http://pdbe.org/6k2o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k2o RCSB], [http://www.ebi.ac.uk/pdbsum/6k2o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k2o ProSAT]</span></td></tr> | ||
| Line 9: | Line 9: | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/E2EA82_9REOV E2EA82_9REOV]] Outer capsid protein VP5*: forms the spike "foot" and "body". Acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment.[SAAS:SAAS00136874] VP8* forms the head of the spikes. It is the viral hemagglutinin and an important target of neutralizing antibodies. In sialic acid-dependent strains, VP8* binds to host cell sialic acid, most probably a ganglioside, providing the initial contact.[SAAS:SAAS00136880] | [[http://www.uniprot.org/uniprot/E2EA82_9REOV E2EA82_9REOV]] Outer capsid protein VP5*: forms the spike "foot" and "body". Acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment.[SAAS:SAAS00136874] VP8* forms the head of the spikes. It is the viral hemagglutinin and an important target of neutralizing antibodies. In sialic acid-dependent strains, VP8* binds to host cell sialic acid, most probably a ganglioside, providing the initial contact.[SAAS:SAAS00136880] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Rotavirus (RV) causes acute gastroenteritis in infants and children worldwide. Recent studies showed that glycans such as histo-blood group antigens (HBGAs) function as cell attachment factors affecting RV host susceptibility and prevalence. P[8] is the predominant RV genotype in humans, but the structural basis of how P[8] RVs interact with glycan ligands remains elusive. In this study, we characterized the interactions between P[8] VP8*s and glycans which showed that VP8*, the RV glycan binding domain, recognized both mucin core 2 and H type 1 antigens according to the ELISA-based oligosaccharide binding assays. Importantly, we determined the structural basis of P[8] RV-glycans interaction from the crystal structures of a Rotateq P[8] VP8* in complex with core 2 and H type 1 glycans at 1.8 A and 2.3 A, respectively, revealing a common binding pocket and similar binding mode. Structural and sequence analysis demonstrated that the glycan binding site is conserved among RVs in the P[II] genogroup, while genotype-specific amino acid variations determined different glycan binding preference. Our data elucidated the detailed structural basis of the interactions between human P[8] RVs and different host glycan factors, shedding light on RV infection, epidemiology, and development of anti-viral agents. | ||
| + | |||
| + | Structural Basis of Glycan Recognition in Globally Predominant Human P[8] Rotavirus.,Sun X, Dang L, Li D, Qi J, Wang M, Chai W, Zhang Q, Wang H, Bai R, Tan M, Duan Z Virol Sin. 2019 Oct 16. pii: 10.1007/s12250-019-00164-7. doi:, 10.1007/s12250-019-00164-7. PMID:31620994<ref>PMID:31620994</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6k2o" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Group a rotaviruses]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Duan, Z]] | [[Category: Duan, Z]] | ||
Revision as of 09:33, 30 October 2019
Structural basis of glycan recognition in globally predominant human P[8] rotavirus
| |||||||||||
