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THE STRUCTURAL BASIS OF THE POOR FIBRIN SPECIFICITY OF UROKINASE(Ⅰ)——KNOWLEDGE-BASED PREDICTION OF KRINGLE STRUCTURES OF UROKINASE AND ITS RELATED PROTEINS
作者姓名:刘建宁  陆樑  高翔  王进  朱德煦  来鲁华  徐筱杰  唐有祺
作者单位:Department of Biochemistry,Nanjing University,Nanjing 210008,PRC,Department of Biochemistry,Nanjing University,Nanjing 210008,PRC,Department of Biochemistry,Nanjing University,Nanjing 210008,PRC,Department of Biochemistry,Nanjing University,Nanjing 210008,PRC,Department of Biochemistry,Nanjing University,Nanjing 210008,PRC,Department of Chemistry,Beijing University,Beijing 100871,PRC,Department of Chemistry,Beijing University,Beijing 100871,PRC,Department of Chemistry,Beijing University,Beijing 100871,PRC
基金项目:This work is supported by the Chinese National High Technology Development Program 863-103-19
摘    要:
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 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.

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