Prediction of the three-dimensional structure of the enzymatic domain of t-PA.
Tissue plasminogen activator (t-PA), an enzyme of the fibrinolytic system, is responsible for lysis of fibrin via activation of plasminogen, and therefore for degradation of blood clots. There are currently no X-ray crystal structure data of the t-PA molecule available either in whole or in part. We therefore predicted the three-dimensional structure of the protease domain by means of computer-graphical methods*. The model obtained forms a basis for understanding the binding of plasminogen to the active site of t-PA. In addition, the interactions of various inhibitors with t-PA were studied by modeling them into the active site. The model also yields an explanation for the observed amidolytic activity of t-PA in the single chain form.
D000595:Amino Acid Sequence; D001665:Binding Sites; D003196:Computer Graphics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010958:Plasminogen; D011487:Protein Conformation; D012697:Serine Endopeptidases; D010959:Tissue Plasminogen Activator
D010958:Plasminogen; D012697:Serine Endopeptidases; D010959:Tissue Plasminogen Activator