1BFW

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

1BFW の概要

• エントリーDOI: 10.2210/pdb1bfw/pdb
• NMR情報: BMRB: 4213
• 分子名称: VP1 PROTEIN (1 entity in total)
• 機能のキーワード: capsid, peptidomimetic, retro-inverso, fmdv, antigen, viral protein
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1973.20

構造登録者

Petit, M.C.,Benkirane, N.,Guichard, G.,Phan Chan Du, A.,Cung, M.T.,Briand, J.P.,Muller, S. (登録日: 1998-05-22, 公開日: 1999-01-13, 最終更新日: 2024-11-20)

主引用文献

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

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: 9920919
DOI: 10.1074/jbc.274.6.3686

実験手法

SOLUTION NMR