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| | <StructureSection load='6k2n' size='340' side='right'caption='[[6k2n]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='6k2n' size='340' side='right'caption='[[6k2n]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6k2n]] is a 6 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=6K2N OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6K2N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6k2n]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Rotavirus_A Rotavirus A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K2N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K2N FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6k2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k2n OCA], [http://pdbe.org/6k2n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k2n RCSB], [http://www.ebi.ac.uk/pdbsum/6k2n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k2n ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</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'>[https://proteopedia.org/fgij/fg.htm?mol=6k2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k2n OCA], [https://pdbe.org/6k2n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k2n RCSB], [https://www.ebi.ac.uk/pdbsum/6k2n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k2n ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == 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] | + | [https://www.uniprot.org/uniprot/E2EA82_9VIRU E2EA82_9VIRU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6k2n" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6k2n" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Group a rotaviruses]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Duan, Z]] | + | [[Category: Rotavirus A]] |
| - | [[Category: Sun, Z]] | + | [[Category: Duan Z]] |
| - | [[Category: Glycan binding specificity]] | + | [[Category: Sun Z]] |
| - | [[Category: Mucin core 2]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| - | [[Category: Vp8* structure]]
| + | |
| Structural highlights
Function
E2EA82_9VIRU
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sun X, Dang L, Li D, Qi J, Wang M, Chai W, Zhang Q, Wang H, Bai R, Tan M, Duan Z. Structural Basis of Glycan Recognition in Globally Predominant Human P[8] Rotavirus. Virol Sin. 2019 Oct 16. pii: 10.1007/s12250-019-00164-7. doi:, 10.1007/s12250-019-00164-7. PMID:31620994 doi:http://dx.doi.org/10.1007/s12250-019-00164-7
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