The crystal structure of the catalytic domain of human urokinase-type plasminogen activator

Background: 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; inhibi...

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Veröffentlicht in:	Structure (London) 1995-07, Vol.3 (7), p.681-691
Hauptverfasser:	Spraggon, Glen, Phillips, Christopher, Nowak, Ursula K, Ponting, Christopher P, Saunders, Derek, Dobson, Christopher M, Stuart, David I, Jones, E.Yvonne
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Binding Sites Chymotrypsin - chemistry Crystallography, X-Ray fibrinolysis Glycosylation Humans inhibitor–protein interaction Models, Molecular Molecular Sequence Data Protein Conformation Protein Structure, Secondary Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Sequence Homology, Amino Acid serine protease Thrombin - chemistry Urokinase-Type Plasminogen Activator - biosynthesis Urokinase-Type Plasminogen Activator - chemistry Urokinase-Type Plasminogen Activator - isolation & purification variable regions X-ray crystallography
Online-Zugang:	Volltext
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