1bfw
RETRO-INVERSO ANALOGUE OF THE G-H LOOP OF VP1 IN FOOT-AND-MOUTH-DISEASE (FMD) VIRUS, NMR, 10 STRUCTURES
|
OverviewOverview
The antigenic activity of a 19-mer peptide corresponding to the major, antigenic region of foot-and-mouth disease virus and its, retro-enantiomeric analogue was found to be completely abolished when they, were tested in a biosensor system in trifluoroethanol. This suggests that, the folding pattern, which is alpha-helix in trifluoroethanol (confirmed, by CD measurement), does not correspond to the biologically relevant, conformation(s) recognized by antibodies. The NMR structures of both, peptides were thus determined in aqueous solution. These studies showed, that the two peptides exhibit similar folding features, particularly in, their C termini. This may explain in part the cross-reactive properties of, the two peptides in aqueous solution. However, the retro-inverso analogue, appears to be more rigid than the parent peptide and contains five, atypical beta-turns. This feature may explain why retro-inverso, foot-and-mouth disease virus peptides are often better recognized than the, parent peptide by anti-virion antibodies.
About this StructureAbout this Structure
1BFW is a Protein complex structure of sequences from [1] with NH2 as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of a retro-inverso peptide analogue mimicking the foot-and-mouth disease virus major antigenic site. Structural basis for its antigenic cross-reactivity with the parent peptide., Petit MC, Benkirane N, Guichard G, Du AP, Marraud M, Cung MT, Briand JP, Muller S, J Biol Chem. 1999 Feb 5;274(6):3686-92. PMID:9920919
Page seeded by OCA on Sun Nov 25 00:08:29 2007