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Structure of Cadherins

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The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins” is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...

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Updated: Jun 5, 2026

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD

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Crystal structure of EHEC intimin: insights into the complementarity between EPEC and EHEC.

Yong Yi¹, Ying Ma, Feng Gao

¹Department of Clinical Microbiology and Clinical Immunology, College of Medical Laboratory, Third Military Medical University, Chongqing, China.

|December 24, 2010

Summary

Structural insights into Enterohaemorrhagic E. coli (EHEC) O157:H7 intimin binding to its receptor Tir were revealed. Variations in EHEC intimin structure influence binding affinity, offering potential for antibacterial drug development.

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Area of Science:

Microbiology
Structural Biology
Pathogen Research

Background:

Enterohaemorrhagic E. coli (EHEC) O157:H7 is a significant foodborne pathogen.
Intimin, a bacterial outer-membrane protein, is crucial for EHEC infection initiation.
Intimin's interaction with its receptor, Tir, is essential for bacterial adhesion and pathogenesis.

Purpose of the Study:

To determine the crystal structure of the Tir-binding domain of EHEC O157:H7 intimin.
To analyze the structural basis of the EHEC intimin-Tir complex.
To compare EHEC intimin structure with that of Enteropathogenic E. coli (EPEC) intimin.

Main Methods:

X-ray crystallography was used to determine the structures of intimin domains.
Structural modeling was employed to build the EHEC intimin-Tir complex.
Comparative structural analysis was performed between EHEC and EPEC intimins.

Main Results:

The crystal structure of the Tir-binding domain of EHEC O157:H7 intimin (Int188) was determined at 2.8 Å resolution.
A structural model of the EHEC intimin-Tir complex revealed key binding residues.
Four significant structural variations were identified between EHEC and EPEC intimins, impacting binding affinities.

Conclusions:

The study provides detailed structural insights into the intimin-Tir binding mechanism in EHEC O157:H7.
Structural differences between EHEC and EPEC intimins explain variations in binding.
Understanding these structural details can inform the development of novel antibacterial strategies targeting EHEC.