Download MendeleyThe crystal structure of the catalytic domain of human urokinase-type plasminogen activator.
Spraggon, G., Phillips, C., Nowak, U.K., Ponting, C.P., Saunders, D., Dobson, C.M., Stuart, D.I., Jones, E.Y.(1995) Structure 3: 681-691
- PubMed: 8591045
- DOI: https://doi.org/10.1016/s0969-2126(01)00203-9
- Primary Citation of Related Structures:
1LMW - PubMed Abstract:
Urokinase-type plasminogen activator (u-PA) promotes fibrinolysis by catalyzing the conversion of plasminogen to the active protease plasmin via the cleavage of a peptide bond. When localized to the external cell surface it contributes to tissue remodelling and cellular migration; inhibition of its activity impedes the spread of cancer. u-PA has three domains: an N-terminal receptor-binding growth factor domain, a central kringle domain and a C-terminal catalytic protease domain. The biological roles of the fibrinolytic enzymes render them therapeutic targets, however, until now no structure of the protease domain has been available. Solution of the structure of the u-PA serine protease was undertaken to provide such data.
Organizational Affiliation:
Laboratory of Molecular Biophysics, Oxford, UK.
