First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.
2qst
From Proteopedia
| 2qst, resolution 2.90Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Gene: | CEACAM5, CEA (Homo sapiens) | ||||||||
| Domains: | V-set | ||||||||
| Related: | 2qsq | ||||||||
| |||||||||
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Crystal structure of the V39C mutant of the N-terminal domain of carcinoembryonic antigen (CEA)
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
2QST is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Korotkova N, Yang Y, Le Trong I, Cota E, Demeler B, Marchant J, Thomas WE, Stenkamp RE, Moseley SL, Matthews S. Binding of Dr adhesins of Escherichia coli to carcinoembryonic antigen triggers receptor dissociation. Mol Microbiol. 2008 Jan;67(2):420-34. Epub 2007 Dec 11. PMID:18086185 doi:10.1111/j.1365-2958.2007.06054.x
Page seeded by OCA on Tue Feb 17 12:08:08 2009
