Structure of an anti-cholera toxin antibody Fab in complex with an epitope-derived D-peptide: a case of polyspecific recognition
| Autor: | Livia Otte, Christa Scholz, Patrick Scheerer, Norbert Krauss, Achim Kramer, Martina Seifert, Jens Schneider-Mergener, Wolfgang Höhne, Helga Wessner |
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| Rok vydání: | 2007 |
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Molecular Cholera Toxin Stereochemistry Molecular Sequence Data Peptide Antigen-Antibody Complex Cross Reactions medicine.disease_cause Crystallography X-Ray Cross-reactivity Epitope Epitopes Immunoglobulin Fab Fragments Mice Structural Biology Antibody Specificity Protein Interaction Mapping medicine Animals Amino Acid Sequence Binding site Tyrosine Molecular Biology chemistry.chemical_classification biology Cholera toxin Amino acid Protein Structure Tertiary Biochemistry chemistry biology.protein Binding Sites Antibody Antibody Peptides |
| Zdroj: | Journal of molecular recognition : JMR. 20(4) |
| ISSN: | 0952-3499 |
| Popis: | The structure of a complex of the anti-cholera toxin antibody TE33 Fab (fragment antibody) with the D-peptide vpGsqhyds was solved to 1.78 A resolution. The D-peptide was derived from the linear L-peptide epitope VPGSQHIDS by a stepwise transformation. Despite the very similar amino acid sequence—the only difference is a tyrosine residue in position 7—there are marked differences in the individual positions with respect to their contribution to the peptide overall affinity as ascertained by a complete substitutional analysis. This is reflected by the X-ray structure of the TE33 Fab/D-peptide complex where there is an inverted orientation of the D-peptide as compared with the known structure of a corresponding complex containing the epitope L-peptide, with the side chains establishing different contacts within the binding site of TE33. The D- and L-peptide affinities are comparable and the surface areas buried by complex formation are almost the same. Thus the antibody TE33 provides a typical example for polyspecific binding behavior of IgG family antibodies. Copyright © 2007 John Wiley & Sons, Ltd. |
| Databáze: | OpenAIRE |
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