Ligand Binding to the Tissue-Type Plasminogen Activator Kringle 2 Domain: Structural Characterization by 1H-NMR

Biochemistry ◽  
1995 ◽  
Vol 34 (9) ◽  
pp. 2739-2750 ◽  
Author(s):  
In-Ja L. Byeon ◽  
Robert F. Kelley ◽  
Michael G. Mulkerrin ◽  
Seong Soo A. An ◽  
Miguel Llinas
Keyword(s):  
Ligand Binding ◽  
Plasminogen Activator ◽  
1H Nmr ◽  
Structural Characterization ◽  
Tissue Type ◽  
Tissue Type Plasminogen Activator ◽  
Type Plasminogen Activator ◽  
Kringle 2

Prion protein stimulates tissue-type plasminogen activator-mediated plasmin generation via a lysine-binding site on kringle 2

2004 ◽  
Vol 2 (6) ◽  
pp. 962-968 ◽  
Author(s):  
Guido Epple ◽  
Wolf-Dieter Schleuning ◽  
Gerhard Kettelgerdes ◽  
Eckart Kottgen ◽  
Reinhard Gessner ◽  
...  
Keyword(s):  
Binding Site ◽  
Plasminogen Activator ◽  
Prion Protein ◽  
Tissue Type ◽  
Tissue Type Plasminogen Activator ◽  
Type Plasminogen Activator ◽  
Kringle 2

Mapping of Epitopes on Human Tissue-Type Plasminogen Activator with Recombinant Deletion Mutant Proteins

1987 ◽  
Vol 57 (01) ◽  
pp. 082-086 ◽  
Author(s):  
Anton-Jan van Zonneveld ◽  
Harry Veerman ◽  
Just P J Brakenhoff ◽  
Lucien A Aarden ◽  
Jean-Francois Cajot ◽  
...  
Keyword(s):  
Plasminogen Activator ◽  
Light Chain ◽  
Deletion Mutant ◽  
Tissue Type ◽  
Mutant Proteins ◽  
Tissue Type Plasminogen Activator ◽  
Type Plasminogen Activator ◽  
Antigen Assay ◽  
Epidermal Growth ◽  
Kringle 2

SummaryAn antigen assay based on a monoclonal antibody directed against the light chain of tissue-type plasminogen activator (t-PA) was developed to quantify seven recombinant (r) t-PA deletion mutant proteins. These recombinant proteins were then employed to map different epitopes on t-PA which interact with a panel of twenty-three monoclonal anti-t-PA antibodies. Twenty were directed against domains on the heavy chain, two against the “finger” domain, three against the “epidermal growth factor-like” domain, five against the kringle 1 domain, and ten against the kringle 2 domain. Only three monoclonal anti-t-PA antibodies interact with the light chain. The finding that the epitopes of each of the monoclonals could be determined with the deletion mutant proteins supports the hypothesis of autonomous folding of structural domains and emphasizes the validity of the use of the recombinant t-PA-deletion mutant proteins for structure-function studies.

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