𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Structure of an anti-cholera toxin antibody Fab in complex with an epitope-derived D-peptide: a case of polyspecific recognition

✍ Scribed by Patrick Scheerer; Achim Kramer; Livia Otte; Martina Seifert; Helga Wessner; Christa Scholz; Norbert Krauß; Jens Schneider-Mergener; Wolfgang Höhne

Publisher
John Wiley and Sons
Year
2007
Tongue
English
Weight
473 KB
Volume
20
Category
Article
ISSN
0952-3499

No coin nor oath required. For personal study only.

✦ Synopsis

Abstract

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 Å 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.

📜 SIMILAR VOLUMES

Bactericidal antibody recognition of a P
Bactericidal antibody recognition of a PorA epitope of Neisseria meningitidis: Crystal structure of a Fab fragment in complex with a fluorescein-conjugated peptide
✍ Jean M.H. van den Elsen; James N. Herron; Peter Hoogerhout; Jan T. Poolman; Edwi 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 197 KB

Class 1 outer membrane protein PorA of Neisseria meningitidis is a vaccine candidate against bacterial meningitis. Antibodies against PorA are able to induce complement-mediated bacterial killing and thereby play an important role in protection against meningococcal disease. Bactericidal antibodies

Solution conformation of an immunogenic
Solution conformation of an immunogenic peptide from HRV2: comparison with the conformation found in a complex with a Fab fragment of an anti-HRV2 neutralizing antibody
✍ M. Antònia Molins; Miquel Àngel Contreras; Ignacio Fita; Miquel Pons 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 175 KB 👁 2 views

The conformation of a [15]-peptide (H-VKAETRLNPDLQPTE-NH 2 ) from VP2 of rhinovirus HRV2 complexed with a Fab fragment was previously shown by X-ray crystallographic studies to be similar to the one found in the corresponding region of HRV1A. Antibodies raised against this peptide bind to and neutra