1bfw
From Proteopedia
(New page: 200px<br /><applet load="1bfw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bfw" /> '''RETRO-INVERSO ANALOGUE OF THE G-H LOOP OF VP...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1bfw.gif|left|200px]]<br /><applet load="1bfw" size=" | + | [[Image:1bfw.gif|left|200px]]<br /><applet load="1bfw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bfw" /> | caption="1bfw" /> | ||
'''RETRO-INVERSO ANALOGUE OF THE G-H LOOP OF VP1 IN FOOT-AND-MOUTH-DISEASE (FMD) VIRUS, NMR, 10 STRUCTURES'''<br /> | '''RETRO-INVERSO ANALOGUE OF THE G-H LOOP OF VP1 IN FOOT-AND-MOUTH-DISEASE (FMD) VIRUS, NMR, 10 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The antigenic activity of a 19-mer peptide corresponding to the major | + | 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== | ==About this Structure== | ||
| - | 1BFW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1BFW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BFW OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Benkirane, N.]] | [[Category: Benkirane, N.]] | ||
| - | [[Category: Briand, J | + | [[Category: Briand, J P.]] |
| - | [[Category: Cung, M | + | [[Category: Cung, M T.]] |
| - | [[Category: Du, A | + | [[Category: Du, A Phan Chan.]] |
[[Category: Guichard, G.]] | [[Category: Guichard, G.]] | ||
[[Category: Muller, S.]] | [[Category: Muller, S.]] | ||
| - | [[Category: Petit, M | + | [[Category: Petit, M C.]] |
[[Category: NH2]] | [[Category: NH2]] | ||
[[Category: antigen]] | [[Category: antigen]] | ||
| Line 26: | Line 26: | ||
[[Category: retro-inverso]] | [[Category: retro-inverso]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:50 2008'' |
Revision as of 09:54, 21 February 2008
|
RETRO-INVERSO ANALOGUE OF THE G-H LOOP OF VP1 IN FOOT-AND-MOUTH-DISEASE (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
1BFW is a Protein complex structure of sequences from [1] with as ligand. 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
Page seeded by OCA on Thu Feb 21 11:54:50 2008
Categories: Protein complex | Benkirane, N. | Briand, J P. | Cung, M T. | Du, A Phan Chan. | Guichard, G. | Muller, S. | Petit, M C. | NH2 | Antigen | Capsid | Fmdv | Peptidomimetic | Retro-inverso
