1ZEA

Structure of the anti-cholera toxin antibody Fab fragment TE33 in complex with a D-peptide

Summary for 1ZEA

• Entry DOI: 10.2210/pdb1zea/pdb
• Related: 1TET
• Descriptor: monoclonal anti-cholera toxin IGG1 KAPPA antibody, L chain, monoclonal anti-cholera toxin IGG1 KAPPA antibody, H chain, short synthetic D-amino acid peptide D2, ... (5 entities in total)
• Functional Keywords: polyspecificity, cross-reactivity, anti-cholera toxin, antigen-antibody complex, antigen recognition, substitution matrix, immune system
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 3
• Total formula weight: 48628.03

Authors

Scheerer, P.,Krauss, N.,Wessner, H.,Scholz, C.,Otte, L.,Seifert, M.,Kramer, A.,Schneider-Mergener, J.,Hoehne, W. (deposition date: 2005-04-18, release date: 2006-04-04, Last modification date: 2024-11-06)

Primary citation

Scheerer, P.,Kramer, A.,Otte, L.,Seifert, M.,Wessner, H.,Scholz, C.,Krauss, N.,Schneider-Mergener, J.,Hohne, W.
Structure of an anti-cholera toxin antibody Fab in complex with an epitope-derived D-peptide: a case of polyspecific recognition.
J.Mol.Recognit., 20:263-274, 2007

PubMed 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 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.

PubMed: 17712773
DOI: 10.1002/jmr.838

Experimental method

X-RAY DIFFRACTION (1.78 Å)