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Assessment of the protein interaction between coagulation factor XII and corn trypsin inhibitor by molecular docking and biochemical validation.

J. Thromb. Haemost.. 2017-09; 
HamadB K, PathakM, MannaR, FischerP M, EmsleyJ, Dekke
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Codon Optimization … A codon-optimized CTI cDNA was obtained from Gen- Script (Piscataway, NJ, USA). High-purity-grade (> 95%) synthetic peptides were obtained from GenScript. Purity was confirmed by reverse-phase HPLC and mass spec- trometry … Get A Quote

摘要

Essentials Corn Trypsin Inhibitor (CTI) is a selective inhibitor of coagulation Factor XII (FXII). Molecular modelling of the CTI-FXIIa complex suggested a canonical inhibitor binding mode. Mutagenesis revealed the CTI inhibitory loop and helices α1 and α2 mediate the interaction. This confirms that CTI inhibits FXII in canonical fashion and validates the molecular model.

关键词

corn trypsin inhibitor,factor XII,molecular docking simulation,serine protease,try