1bfw

RETRO-INVERSO ANALOGUE OF THE G-H LOOP OF VP1 IN FOOT-AND-MOUTH-DISEASE (FMD) VIRUS, NMR, 10 STRUCTURES

spinqualitylabelsall models 1bfw, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1bfw is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: DAL, DAR, DAS, DGN, DLE, DPN, DPR, DSN, DVA, LML, NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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