2qst
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Carcinoembryonic antigen (CEA)-related cell adhesion molecules (CEACAMs) | + | 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== | ==About this Structure== | ||
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==Reference== | ==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 | + | 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. 2008 Jan;67(2):420-34. Epub 2007 Dec 11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18086185 18086185] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Korotkova, N.]] | [[Category: Korotkova, N.]] | ||
| - | [[Category: Moseley, S | + | [[Category: Moseley, S L.]] |
| - | [[Category: Stenkamp, R | + | [[Category: Stenkamp, R E.]] |
| - | [[Category: Trong, I | + | [[Category: Trong, I Le.]] |
[[Category: cell adhesion]] | [[Category: cell adhesion]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
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[[Category: polymorphism]] | [[Category: polymorphism]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:41:57 2008'' |
Revision as of 16:41, 21 February 2008
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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. 2008 Jan;67(2):420-34. Epub 2007 Dec 11. PMID:18086185
Page seeded by OCA on Thu Feb 21 18:41:57 2008
