1zea

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spinqualitylabelsall models 1zea, resolution 1.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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 (c) 2007 John Wiley & Sons, Ltd.

About this Structure

1ZEA is a Protein complex structure of sequences from Mus musculus with CIT as ligand. Full crystallographic information is available from OCA.

Reference

Structure of an anti-cholera toxin antibody Fab in complex with an epitope-derived D-peptide: a case of polyspecific recognition., Scheerer P, Kramer A, Otte L, Seifert M, Wessner H, Scholz C, Krauss N, Schneider-Mergener J, Hohne W, J Mol Recognit. 2007 Jul;20(4):263-274. PMID:17712773

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