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PDBsum entry 5jdb

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protein Protein-protein interface(s) links
Viral protein PDB id
5jdb

 

 

 

 

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Contents
Protein chains
(+ 0 more) 160 a.a.
Waters ×483
PDB id:
5jdb
Name: Viral protein
Title: Binding specificity of p[8] vp8 Proteins of rotavirus vaccine strains with histo-blood group antigens
Structure: Outer capsid protein vp4. Chain: a, b, c, d, e, f. Fragment: unp residues 64-223. Engineered: yes
Source: Rotavirus a. Organism_taxid: 28875. Expressed in: escherichia coli k-12. Expression_system_taxid: 83333.
Resolution:
1.90Å     R-factor:   0.204     R-free:   0.230
Authors: X.Sun,N.Guo,D.Li,Y.Zhou,M.Jin,G.Xie,L.Pang,Q.Zhang,Y.Cao,Z.Duan
Key ref: X.Sun et al. (2016). Binding specificity of P[8] VP8* proteins of rotavirus vaccine strains with histo-blood group antigens. Virology, 495, 129-135. PubMed id: 27209447 DOI: 10.1016/j.virol.2016.05.010
Date:
16-Apr-16     Release date:   13-Jul-16    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
E2EA82  (E2EA82_9VIRU) -  Outer capsid protein VP4 from Rotavirus A
Seq:
Struc:
 
Seq:
Struc:
775 a.a.
160 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1016/j.virol.2016.05.010 Virology 495:129-135 (2016)
PubMed id: 27209447  
 
 
Binding specificity of P[8] VP8* proteins of rotavirus vaccine strains with histo-blood group antigens.
X.Sun, N.Guo, D.Li, M.Jin, Y.Zhou, G.Xie, L.Pang, Q.Zhang, Y.Cao, Z.J.Duan.
 
  ABSTRACT  
 
RotaTeq(®) 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 1.9Å. 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.
 

 

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