2VER

Structural model for the complex between the Dr adhesins and carcinoembryonic antigen (CEA)

2VER の概要

• エントリーDOI: 10.2210/pdb2ver/pdb
• 関連するPDBエントリー: 1E07 1RXL 1USZ 1UT2 2IXQ
• 分子名称: AFIMBRIAL ADHESIN AFA-III, ARCINOEMBRYONIC ANTIGEN-RELATED CELL ADHESION MOLECULE 5, S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate (3 entities in total)
• 機能のキーワード: membrane, fimbrium, gpi-anchor, lipoprotein, immunoglobulin domain, cell adhesion, cell projection
• 由来する生物種: ESCHERICHIA COLI; 詳細
• 細胞内の位置: Fimbrium: Q57254; Cell membrane; Lipid-anchor, GPI-anchor: P06731
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28564.12

構造登録者

Korotkova, N.,Yang, Y.,Le Trong, I.,Cota, E.,Demeler, B.,Marchant, J.,Thomas, W.E.,Stenkamp, R.E.,Moseley, S.L.,Matthews, S. (登録日: 2007-10-26, 公開日: 2008-01-08, 最終更新日: 2011-07-13)

主引用文献

Korotkova, N.,Yang, Y.,Le Trong, I.,Cota, E.,Demeler, B.,Marchant, J.,Thomas, W.E.,Stenkamp, R.E.,Moseley, S.L.,Matthews, S.
Binding of Dr Adhesins of Escherichia Coli to Carcinoembryonic Antigen Triggers Receptor Dissociation.
Mol.Microbiol., 67:420-, 2008

PubMed Abstract: 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.

PubMed: 18086185
DOI: 10.1111/J.1365-2958.2007.06054.X

実験手法

SOLUTION NMR