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| | ==Crystal Structure of FAB F22-4 in complex with a Carbohydrate-mimetic peptide== | | ==Crystal Structure of FAB F22-4 in complex with a Carbohydrate-mimetic peptide== |
| - | <StructureSection load='3ggw' size='340' side='right' caption='[[3ggw]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='3ggw' size='340' side='right'caption='[[3ggw]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ggw]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GGW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GGW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ggw]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GGW FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3c5s|3c5s]], [[3bz4|3bz4]], [[3c6s|3c6s]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ggw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ggw OCA], [http://pdbe.org/3ggw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ggw RCSB], [http://www.ebi.ac.uk/pdbsum/3ggw PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ggw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ggw OCA], [https://pdbe.org/3ggw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ggw RCSB], [https://www.ebi.ac.uk/pdbsum/3ggw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ggw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
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| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gg/3ggw_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gg/3ggw_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | ==See Also== | | ==See Also== |
| - | *[[Antibody|Antibody]] | + | *[[Antibody 3D structures|Antibody 3D structures]] |
| | + | *[[3D structures of non-human antibody|3D structures of non-human antibody]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| - | [[Category: Bentley, G A]] | + | [[Category: Bentley GA]] |
| - | [[Category: Normand, B Vulliez-Le]]
| + | [[Category: Saul FA]] |
| - | [[Category: Saul, F A]] | + | [[Category: Vulliez-Le Normand B]] |
| - | [[Category: Antibody complex]] | + | |
| - | [[Category: Immune system]]
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| - | [[Category: Lp]]
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| - | [[Category: Peptide-carbohydrate mimicry]]
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| - | [[Category: Shigella flexneri]]
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| Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The use of carbohydrate-mimicking peptides to induce immune responses against surface polysaccharides of pathogenic bacteria offers a novel approach to vaccine development. Factors governing antigenic and immunogenic mimicry, however, are complex and poorly understood. We have addressed this question using the anti-lipopolysaccharide monoclonal antibody F22-4, which was raised against Shigella flexneri serotype 2a and shown to protect against homologous infection in a mouse model. In a previous crystallographic study, we described F22-4 in complex with two synthetic fragments of the O-antigen, the serotype-specific saccharide moiety of lipopolysaccharide. Here, we present a crystallographic and NMR study of the interaction of F22-4 with a dodecapeptide selected by phage display using the monoclonal antibody. Like the synthetic decasaccharide, the peptide binds to F22-4 with micromolar affinity. Although the peptide and decasaccharide use very similar regions of the antigen-binding site, indicating good antigenic mimicry, immunogenic mimicry by the peptide was not observed. The F22-4-antigen interaction is significantly more hydrophobic with the peptide than with oligosaccharides; nonetheless, all hydrogen bonds formed between the peptide and F22-4 have equivalents in the oligosaccharide complex. Two bridging water molecules are also in common, adding to partial structural mimicry. Whereas the bound peptide is entirely helical, its structure in solution, as shown by NMR, is helical in the central region only. Moreover, docking the NMR structure into the antigen-binding site shows that steric hindrance would occur, revealing poor complementarity between the major solution conformation and the antibody that could contribute to the absence of immunogenic mimicry.
Structural mimicry of O-antigen by a peptide revealed in a complex with an antibody raised against Shigella flexneri serotype 2a.,Theillet FX, Saul FA, Vulliez-Le Normand B, Hoos S, Felici F, Weintraub A, Mulard LA, Phalipon A, Delepierre M, Bentley GA J Mol Biol. 2009 May 15;388(4):839-50. Epub 2009 Mar 27. PMID:19328810[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Theillet FX, Saul FA, Vulliez-Le Normand B, Hoos S, Felici F, Weintraub A, Mulard LA, Phalipon A, Delepierre M, Bentley GA. Structural mimicry of O-antigen by a peptide revealed in a complex with an antibody raised against Shigella flexneri serotype 2a. J Mol Biol. 2009 May 15;388(4):839-50. Epub 2009 Mar 27. PMID:19328810 doi:10.1016/j.jmb.2009.03.057
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