The refined 1.9-Å X-ray crystal structure of d-Phe-Pro-Arg chloromethylketone-inhibited humanα-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships

Author:

Bode Wolfram,Turk Dusan,Karshikov Andrej

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference201 articles.

1. Binding of the bovine basic pancreatic trypsin inhibitor (Kunitz) to human α-, β- and γ-thrombin; a kinetic and thermodynamic study;Ascenzi;Biochim. Biophys. Acta,1988

2. Inhibition of thrombin and trypsin by tripeptide aldehydes;Bajusz;Int. J. Peptide Protein Res.,1978

3. Highly active and selective anticoagulants: d-Phe-Pro-Arg-H, a free tripeptide aldehyde prone to spontaneous inactivation, and its stable N-methyl derivative, d-Me-Phe-Pro-Arg-H;Bajusz;J. Mol. Chem.,1990

4. Binding of thrombin to subendothelial extracellular matrix; protection and expression of functional properties;Bar-Shavit;J. Clin. Invest.,1989

5. Growth-promoting effects of esterolytically inactive thrombin on macrophages;Bar-Shavit;Cell Biochem.,1986

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