View source for 5jdb


==Binding specificity of P[8] VP8* proteins of rotavirus vaccine strains with histo-blood group antigens==
<StructureSection load='5jdb' size='340' side='right'caption='[[5jdb]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5jdb]] 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=5JDB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JDB 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]] 1.901&#8491;</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=5jdb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jdb OCA], [https://pdbe.org/5jdb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jdb RCSB], [https://www.ebi.ac.uk/pdbsum/5jdb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jdb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E2EA82_9VIRU E2EA82_9VIRU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
RotaTeq((R)) and Rotarix are two common human rotavirus (RV) vaccines currently on the market worldwide. Recent studies indicate histo-blood group antigens (HBGAs) may be attachment factors for RVs. The P[8] VP8* proteins of RotaTeq and Rotarix were expressed and purified, and their binding specificities were evaluated. Saliva-based binding assays showed that the VP8* proteins bound to the saliva samples of secretors irrespective of ABO blood types. However, in the oligosaccharide binding assay, the VP8* proteins displayed no specific binding to the HBGAs tested, including Lewis b and H1. The structure of RotaTeq P[8] VP8* was solved at 1.9A. Structural comparisons revealed that the putative receptor binding site was different to that of other genotypes and displayed a novel potential binding region. These findings indicate RotaTeq and Rotarix may have better efficiency in areas with a high percentage of secretors.

Binding specificity of P[8] VP8* proteins of rotavirus vaccine strains with histo-blood group antigens.,Sun X, Guo N, Li D, Jin M, Zhou Y, Xie G, Pang L, Zhang Q, Cao Y, Duan ZJ Virology. 2016 Aug;495:129-35. doi: 10.1016/j.virol.2016.05.010. Epub 2016 May, 19. PMID:27209447<ref>PMID:27209447</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5jdb" 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: Rotavirus A]]
[[Category: Cao Y]]
[[Category: Duan Z]]
[[Category: Guo N]]
[[Category: Jin M]]
[[Category: Li D]]
[[Category: Pang L]]
[[Category: Sun X]]
[[Category: Xie G]]
[[Category: Zhang Q]]
[[Category: Zhou Y]]