2qst
From Proteopedia
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Crystal structure of the V39C mutant of the N-terminal domain of carcinoembryonic antigen (CEA)
Overview
Carcinoembryonic antigen (CEA)-related cell adhesion molecules (CEACAMs), are host receptors for the Dr family of adhesins of Escherichia coli. To, define the mechanism for binding of Dr adhesins to CEACAM receptors, we, carried out structural studies on the N-terminal domain of CEA and its, complex with the Dr adhesin. The crystal structure of CEA reveals a dimer, similar to other dimers formed by receptors with IgV-like domains. The, structure of the CEA/Dr adhesin complex is proposed based on NMR, spectroscopy and mutagenesis data in combination with biochemical, characterization. The Dr adhesin/CEA interface overlaps appreciably with, the region responsible for CEA dimerization. Binding kinetics, mutational, analysis and spectroscopic examination of CEA dimers suggest that Dr, adhesins can dissociate CEA dimers prior to the binding of monomeric, forms. Our conclusions include a plausible mechanism for how E. coli, and, perhaps other bacterial and viral pathogens, exploit CEACAMs. The present, structure of the complex provides a powerful tool for the design of novel, inhibitory strategies to treat E. coli infections.
About this Structure
2QST is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Binding of Dr adhesins of Escherichia coli to carcinoembryonic antigen triggers receptor dissociation., Korotkova N, Yang Y, Le Trong I, Cota E, Demeler B, Marchant J, Thomas WE, Stenkamp RE, Moseley SL, Matthews S, Mol Microbiol. 2007 Dec 11;. PMID:18086185
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