|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5vx4' size='340' side='right'caption='[[5vx4]], [[Resolution|resolution]] 1.55Å' scene=''> | | <StructureSection load='5vx4' size='340' side='right'caption='[[5vx4]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5vx4]] 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=5VX4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VX4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5vx4]] is a 1 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=5VX4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VX4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 1.55Å</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=5vx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vx4 OCA], [http://pdbe.org/5vx4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vx4 RCSB], [http://www.ebi.ac.uk/pdbsum/5vx4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vx4 ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=5vx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vx4 OCA], [https://pdbe.org/5vx4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vx4 RCSB], [https://www.ebi.ac.uk/pdbsum/5vx4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vx4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q2VE61_9REOV Q2VE61_9REOV]] Outer capsid protein VP5*: Forms the spike "foot" and "body" and acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. This reorganization may be linked to membrane penetration by exposing VP5* hydrophobic region. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment.[SAAS:SAAS01043052] | + | [https://www.uniprot.org/uniprot/Q2VE61_9VIRU Q2VE61_9VIRU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 18: |
Line 19: |
| | </div> | | </div> |
| | <div class="pdbe-citations 5vx4" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5vx4" 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: Hu, L]] | + | [[Category: Rotavirus A]] |
| - | [[Category: Prasad, B V.Venkataram]] | + | [[Category: Hu L]] |
| - | [[Category: Glycan]] | + | [[Category: Venkataram Prasad BV]] |
| - | [[Category: Hbga]]
| + | |
| - | [[Category: Rotavirus]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
Q2VE61_9VIRU
Publication Abstract from PubMed
Rotaviruses (RVs) cause life-threatening diarrhea in infants and children worldwide. Recent biochemical and epidemiological studies underscore the importance of histo-blood group antigens (HBGA) as both cell attachment and susceptibility factors for the globally dominant P[4], P[6], and P[8] genotypes of human RVs. How these genotypes interact with HBGA is not known. Here, our crystal structures of P[4] and a neonate-specific P[6] VP8*s alone and in complex with H-type I HBGA reveal a unique glycan binding site that is conserved in the globally dominant genotypes and allows for the binding of ABH HBGAs, consistent with their prevalence. Remarkably, the VP8* of P[6] RVs isolated from neonates displays subtle structural changes in this binding site that may restrict its ability to bind branched glycans. This provides a structural basis for the age-restricted tropism of some P[6] RVs as developmentally regulated unbranched glycans are more abundant in the neonatal gut.
Glycan recognition in globally dominant human rotaviruses.,Hu L, Sankaran B, Laucirica DR, Patil K, Salmen W, Ferreon ACM, Tsoi PS, Lasanajak Y, Smith DF, Ramani S, Atmar RL, Estes MK, Ferreon JC, Prasad BVV Nat Commun. 2018 Jul 6;9(1):2631. doi: 10.1038/s41467-018-05098-4. PMID:29980685[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hu L, Sankaran B, Laucirica DR, Patil K, Salmen W, Ferreon ACM, Tsoi PS, Lasanajak Y, Smith DF, Ramani S, Atmar RL, Estes MK, Ferreon JC, Prasad BVV. Glycan recognition in globally dominant human rotaviruses. Nat Commun. 2018 Jul 6;9(1):2631. doi: 10.1038/s41467-018-05098-4. PMID:29980685 doi:http://dx.doi.org/10.1038/s41467-018-05098-4
|
