1TET

CRYSTAL STRUCTURE OF AN ANTICHOLERA TOXIN PEPTIDE COMPLEX AT 2.3 ANGSTROMS

Summary for 1TET

• Entry DOI: 10.2210/pdb1tet/pdb
• Descriptor: IGG1 TE33 FAB (LIGHT CHAIN), IGG1 TE33 FAB (HEAVY CHAIN), CHOLERA TOXIN PEPTIDE 3 (CTP3), ... (5 entities in total)
• Functional Keywords: immunoglobulin
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 3
• Total formula weight: 48496.12

Authors

Shoham, M. (deposition date: 1993-06-21, release date: 1994-01-31, Last modification date: 2024-11-20)

Primary citation

Shoham, M.
Crystal structure of an anticholera toxin peptide complex at 2.3 A.
J.Mol.Biol., 232:1169-1175, 1993

PubMed Abstract: 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.

PubMed: 7690406
DOI: 10.1006/jmbi.1993.1469

Experimental method

X-RAY DIFFRACTION (2.3 Å)