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Domain structure of hepatocyte growth factor/scatter factor (HGF/SF)
E Gherardi1, G Hartmann, J Hepple
1Cambridge University Medical School, MRC Centre, UK.
Ciba Foundation Symposium
|January 1, 1997
Summary
Hepatocyte growth factor/scatter factor (HGF/SF) domain deletions reveal essential regions for activity. Truncated variants (NK1, NK2) show varied HGF/SF agonistic or antagonistic effects, guiding future structural studies.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- Hepatocyte growth factor/scatter factor (HGF/SF) possesses a modular structure crucial for its biological functions.
- Understanding the structure-function relationship of HGF/SF is key to elucidating its role in cellular processes.
Purpose of the Study:
- To analyze the structure-function relationship of HGF/SF through domain deletion and structural modeling.
- To investigate the activity of truncated HGF/SF variants (NK1, NK2) and their potential agonistic or antagonistic roles.
Main Methods:
- Domain deletion experiments were performed to identify essential HGF/SF domains for target cell activity.
- Three-dimensional (3D) structures of HGF/SF domains were modeled based on homologous structures.
- Protein engineering techniques are being used to assess predictions from structural models.
Main Results:
- The N-domain, kringle 1, and kringle 2 of HGF/SF are essential for its activity on target cells.
- Truncated variants, NK1 (N-domain and kringle 1) and NK2 (kringles 1 and 2), exhibit partial agonistic or antagonistic activity.
- This activity is dependent on the target cells and the presence of full-length HGF/SF.
Conclusions:
- The modularity of HGF/SF allows for distinct functional roles of its domains.
- Truncated HGF/SF variants offer insights into receptor binding and activation mechanisms.
- Structural modeling and experimental validation are crucial for a comprehensive understanding of HGF/SF function.