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Urokinase-Type Plasminogen
Activator
Urokinase-type plasminogen activator is a strong plasminogen activator which
specifically cleaves the proenzyme/zymogen plasminogen to form the active enzyme
plasmin. It specifically catalyzes the cleavage of the arg-|-val bond in
plasminogen. The active plasmin is then able to break down the fibrin polymers
of blood clots. Clinically, urokinase-type plasminogen activator is given to
patients suffering from thrombolytic disorders.
The amino terminal fragment (ATF) of urokinase-type plasminogen activator is 130
amino acid residues long. It consists of 2 alpha-helices (green) and 2
antiparallel beta-strands (purple). The ATF contains 2 domains; a growth factor
domain and a kringle domain. It binds fucose (magenta) as a ligand. Fucose is a
deoxy sugar, a monosaccharide with one or more hydroxyl (-OH) groups replaced by
a hydrogen (-H). The formula for fucose is C6H12O6.
The ATF also contains 6 disulfide bonds (blue) and are as follows: Cys11-Cys19,
Cys13-Cys31, Cys33-Cys42, Cys50-Cys131, Cys71-Cys113, and Cys102-Cys126.
- Keywords: Plasminogen
Activation, Hydrolase, Serine Protease, Glycoprotein, Kringle, EGF-Like
Domain, Zymogen, Signal, Polymorphism
- View this protein's PDB entry
as 1URK
- View this protein's SwissProt
entry as UROK_HUMAN
- References:
- A.P. Hansen, A.M.
Petros, R.P. Meadows, D.G. Nettesheim, A.P. Mazar, E.T. Olejniczak, R.X.
Xu, T.M. Pederson, J. Henkin, S.W. Fesik
Solution Structure of the Amino Terminal Fragment of Urokinase-Type
Plasminogen Activator.
Biochemistry 33:4847 (1994)
http://www-nmr.cabm.rutgers.edu/~gardino/page33.html
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