1tet
From Proteopedia
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CRYSTAL STRUCTURE OF AN ANTICHOLERA TOXIN PEPTIDE COMPLEX AT 2.3 ANGSTROMS
Overview
Cholera toxin peptide 3 (CTP3) is a 15-residue peptide corresponding in, sequence to an immunogenic loop on the surface of the B-subunits of both, cholera toxin and the heat-labile toxin from Escherichia coli. TE33 is the, Fab fragment of a monoclonal antibody elicited against CTP3. The crystal, structure of the TE33-CTP3 complex at 2.3 A resolution reveals an, antigen-binding pocket, 13 A deep and 13 A wide, which is lined with many, aromatic residues. The N-terminal portion of the peptide antigen CTP3, forms a type II beta-turn that fits snugly into this pocket. At gln7 the, peptide backbone of CTP3 forms a kink followed by an extended C-terminal, chain that seals off the cleft and buries the beta-turn underneath it. All, six complementarity-determining regions of TE33 contribute to the binding, of CTP3. The antibody-peptide contacts include, in addition to van der, Waals' interactions and hydrogen bonds, also one salt bridge and one water, molecule, which mediates the interaction.
About this Structure
1TET is a Protein complex structure of sequences from Mus musculus with CIT as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of an anticholera toxin peptide complex at 2.3 A., Shoham M, J Mol Biol. 1993 Aug 20;232(4):1169-75. PMID:7690406
Page seeded by OCA on Sun Nov 25 02:06:04 2007
