1BFW
RETRO-INVERSO ANALOGUE OF THE G-H LOOP OF VP1 IN FOOT-AND-MOUTH-DISEASE (FMD) VIRUS, NMR, 10 STRUCTURES
Summary for 1BFW
| Entry DOI | 10.2210/pdb1bfw/pdb |
| NMR Information | BMRB: 4213 |
| Descriptor | VP1 PROTEIN (1 entity in total) |
| Functional Keywords | capsid, peptidomimetic, retro-inverso, fmdv, antigen, viral protein |
| Total number of polymer chains | 1 |
| Total formula weight | 1973.20 |
| Authors | Petit, M.C.,Benkirane, N.,Guichard, G.,Phan Chan Du, A.,Cung, M.T.,Briand, J.P.,Muller, S. (deposition date: 1998-05-22, release date: 1999-01-13, Last modification date: 2024-11-20) |
| Primary citation | Petit, M.C.,Benkirane, N.,Guichard, G.,Du, A.P.,Marraud, M.,Cung, M.T.,Briand, J.P.,Muller, S. 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. J.Biol.Chem., 274:3686-3692, 1999 Cited by PubMed Abstract: 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. PubMed: 9920919DOI: 10.1074/jbc.274.6.3686 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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