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Implications of atomic-resolution structures for cell adhesion
1Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA. leahy@groucho.med.jhmi.edu
Annual Review of Cell and Developmental Biology
|January 1, 1997
Summary
High-resolution structures of cell adhesion molecules reveal ligand and metal-binding sites, aiding drug design and evolutionary studies. These insights enhance understanding of molecular interactions in cell adhesion processes.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- Cell adhesion molecules are modular, with domains belonging to large protein families.
- Recent high-resolution structures of integrins, cadherins, and other adhesion molecules have been determined.
Purpose of the Study:
- To review recently determined structures of cell adhesion molecules.
- To summarize key findings from these structures.
- To highlight common features across different cell adhesion systems.
Main Methods:
- X-ray crystallography and other high-resolution structural determination techniques.
- Analysis of structural data to identify ligand- and metal-binding sites.
- Comparative analysis of structures to understand evolutionary relationships.
Main Results:
- Visualization of ligand-binding sites, providing insights into molecular interactions.
- Identification and characterization of metal-binding sites, clarifying the role of ions.
- Structures serve as templates for modeling homologous domains and multidomain arrays.
- Revealed unexpected relationships, prompting questions about domain evolution.
Conclusions:
- High-resolution structures significantly advance the understanding of cell adhesion mechanisms.
- Structural information facilitates rational drug design targeting specific binding sites.
- These structures offer valuable insights into the evolutionary origins of protein domains.