The structural basis of the poor fibrin specificity of urokinase(I)--knowledge-based prediction of kringle structures of urokinase and its related proteins.
The Kringle-1 structure of plasminogen (PGK-1), the Kringle-2 structure of tissue plasminogen activator (PAK-2) and the Kringle structure of prourokinase (UKK) has been modeled on the basis of the three-dimensional structure of Kringle-1 of prothrombin (PTK-1) at 2.8 A resolution. The predicted three-dimensional structure of these Kringles shows that the binding site of PGK-1 is characterized by an apparent dipolar site, the polar parts of which are separated by a hydrophobic region. PAK-2 possesses the anionic center but has not a cationic binding center which might be provided by a guanidinium group from Arg-69 located adjacent to the Arg-71 position. UKK possesses neither the anionic binding center nor the cationic center which are probably the main reason for the poor fibrin specificity of urokinase.
Liu
J N
JN
Department of Biochemistry, Nanjing University, PRC.
Lu
L
L
Gao
X
X
Wang
J
J
Zhu
D X
DX
Lai
L H
LH
Xu
X J
XJ
Tang
Y Q
YQ
D000595:Amino Acid Sequence; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D010959:Tissue Plasminogen Activator / Q000235:genetics; D014568:Urokinase-Type Plasminogen Activator / Q000235:genetics*
D010959:Tissue Plasminogen Activator; D014568:Urokinase-Type Plasminogen Activator