The solution structure and backbone dynamics of the fibronectin type I and epidermal growth factor-like pair of modules of tissue-type plasminogen activator.
Smith, B.O., Downing, A.K., Driscoll, P.C., Dudgeon, T.J., Campbell, I.D.(1995) Structure 3: 823-833
- PubMed: 7582899 
- DOI: https://doi.org/10.1016/s0969-2126(01)00217-9
- Primary Citation of Related Structures:  
1TPG - PubMed Abstract: 
The thrombolytic serine protease tissue-type plasminogen activator (t-PA) is a classical modular protein consisting of three types of domain in addition to the serine protease domain: F1 (homologous to fibronectin type I); G (epidermal growth factor-like) and kringle. Biochemical data suggest that the F1 and G modules play a major role in the binding of t-PA to fibrin and to receptors on hepatocytes.
Organizational Affiliation: 
Oxford Centre for Molecular Sciences, UK.