1bcv
From Proteopedia
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|PDB= 1bcv |SIZE=350|CAPTION= <scene name='initialview01'>1bcv</scene> | |PDB= 1bcv |SIZE=350|CAPTION= <scene name='initialview01'>1bcv</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bcv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bcv OCA], [http://www.ebi.ac.uk/pdbsum/1bcv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bcv RCSB]</span> | ||
}} | }} | ||
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[[Category: Muller, S.]] | [[Category: Muller, S.]] | ||
[[Category: Petit, M C.]] | [[Category: Petit, M C.]] | ||
| - | [[Category: ACE]] | ||
[[Category: antigene]] | [[Category: antigene]] | ||
[[Category: synthetic peptide]] | [[Category: synthetic peptide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:58:17 2008'' |
Revision as of 15:58, 30 March 2008
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SYNTHETIC PEPTIDE CORRESPONDING TO THE MAJOR IMMUNOGEN SITE OF FMD VIRUS, NMR, 10 STRUCTURES
Overview
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 Structure
1BCV is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
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
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