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Three-dimensional structural analysis of fibronectin heparin-binding domain mutations
1Department of Stomatology, University of California-San Francisco, San Francisco, CA 94143-0512, USA. ykapila@itsa.ucsf.edu
Journal of Cellular Biochemistry. Supplement
|July 17, 2001
Summary
Two point mutations in fibronectin
Area of Science:
- Biochemistry
- Cell Biology
- Structural Biology
Background:
- Fibronectin's V region and heparin-binding domain influence tumor cell invasion, proteinase expression, and apoptosis.
- A cationic cradle in fibronectin domain III-13, formed by specific residues, binds heparin.
Purpose of the Study:
- To investigate if two engineered point mutations in fibronectin's heparin-binding domain alter the cationic cradle's conformation.
- To understand how these mutations affect cell behavior.
Main Methods:
- Constructed a three-dimensional model of fibronectin domain III-13 using a homologous tenascin domain template.
- Replaced differing amino acid sequences and substituted specific arginine residues with threonine.
Main Results:
- The model showed mutated threonine residues are solvent accessible and accommodated within the beta strand.
- The mutated residues remained integral to the three-dimensional cationic cradle structure.
Conclusions:
- The two point mutations in fibronectin domain III-13 likely alter cell function through charge modifications rather than conformational changes to the heparin-binding cradle.