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Domain structure and organisation in extracellular matrix proteins
Erhard Hohenester1, Jürgen Engel
1Department of Biological Sciences, Biophysics Section, Blackett Laboratory, Imperial College, Prince Consort Road, London SW7 2BW, UK. e.hohenester@ic.ac.uk
Matrix Biology : Journal of the International Society for Matrix Biology
|February 20, 2002
Summary
Recent advances in understanding extracellular matrix (ECM) protein structure reveal principles of higher-order architecture and ligand binding. Structural insights are crucial for elucidating the biological functions of these complex protein molecules.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- Extracellular matrix (ECM) proteins are modular, assembled from distinct domains.
- Understanding ECM protein structure is key to their biological function.
Purpose of the Study:
- To review recent advances in ECM protein structure determination.
- To highlight how structural information illuminates ECM protein function.
Main Methods:
- X-ray crystallography and NMR spectroscopy to determine domain structures.
- Analysis of domain pairs, tandem arrays, and oligomerization domains.
- Site-directed mutagenesis to study domain cooperation.
Main Results:
- Basic folds of many ECM domains are known.
- Principles of higher-order ECM protein architecture are emerging.
- Structural data explains cooperative ligand binding between domains.
Conclusions:
- Structural studies provide critical insights into ECM protein assembly and function.
- Recent structural data on heterotypic ECM complexes are advancing the field.