publication . Article . 2017

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

B. K. Hamad; M. Pathak; R. Manna; P. M. Fischer; J. Emsley; L. V. Dekker;
Open Access English
  • Published: 09 Aug 2017 Journal: Journal of Thrombosis and Haemostasis, volume 15, issue 9, pages 1,818-1,828 (issn: 1538-7933, eissn: 1538-7836, Copyright policy)
  • Publisher: John Wiley and Sons Inc.
  • Country: Italy
Abstract
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. Summary Background Corn trypsin inhibitor (CTI) has selectivity for the serine proteases coagulation factor XII and trypsin. CTI is in widespread use as a reagent that specifically inhibits the intrinsic pathway of blood coagulation but not the extrinsic pathway. Objectives To investigate the mole...
Subjects
free text keywords: Original Article, COAGULATION, Original Articles, corn trypsin inhibitor, factor XII, molecular docking simulation, serine protease, trypsin, factor XII, Hematology, Biochemistry, biology.protein, biology, Salt bridge, Serine, medicine.drug, medicine, business.industry, business, Coagulation Factor XII, Protease, medicine.medical_treatment, Docking (molecular)
Related Organizations
48 references, page 1 of 4

1 Stavrou E, Schmaier AH. Factor XII: what does it contribute to our understanding of the physiology and pathophysiology of hemostasis & thrombosis. Thromb Res 2010; 125: 210–15.20022081 [OpenAIRE] [PubMed]

2 Henriques ES, Floriano WB, Reuter N, Melo A, Brown D, Gomes JANF, Maigret B, Nascimento MAC, Ramos MJ. The search for a new model structure of b‐Factor XIIa. J Comput Aided Mol Des 2001; 15: 309–22.11349814 [PubMed]

3 Pathak M, Wilmann P, Awford J, Li C, Hamad BK, Fischer PM, Dreveny I, Dekker LV, Emsley J. Coagulation factor XII protease domain crystal structure. J Throm b Haemost 2015; 13: 580–91.25604127 [OpenAIRE] [PubMed]

4 Citarella F, Ravon DM, Pascucci B, Felici A, Fantoni A, Hack CE. Structure/function analysis of human factor XII using recombinant deletion mutants. Evidence for an additional region involved in the binding to negatively charged surfaces. Eur J Biochem 1996; 238: 240–9.8665943 [OpenAIRE] [PubMed]

5 Iwaki T, Castellino FJ. Plasma levels of bradykinin are suppressed in factor XII‐deficient mice. Thromb Haemost 2006; 95: 1003–10.16732380 [OpenAIRE] [PubMed]

6 Emsley J, McEwan PA, Gailani D. Structure and function of factor XI. Blood 2010; 115: 2569–77.20110423 [OpenAIRE] [PubMed]

7 Pauer HU, Renne T, Hemmerlein B, Legler T, Fritzlar S, Adham I, Muller‐Esterl W, Emons G, Sancken U, Engel W, Burfeind P. Targeted deletion of murine coagulation factor XII gene – a model for contact phase activation in vivo . Thromb Haemost 2004; 92: 503–8.15351846 [PubMed]

8 Renne T, Pozgajova M, Gruner S, Schuh K, Pauer HU, Burfeind P, Gailani D, Nieswandt B. Defective thrombus formation in mice lacking coagulation factor XII. J Exp Med 2005; 202: 271–81.16009717 [OpenAIRE] [PubMed]

9 Ng TB. Naturally occurring anti‐insect proteins: current status and future aspects In: Rai M, Carpinella MC, eds. Naturally Occurring Bioactive Compounds. Amsterdam: Elsevier, 2006: 409–10.

10 Lei MG, Reeck GR. Combined use of trypsin‐agarose affin ity chromatography and reversed‐phase high‐performance liquid chromatography for the purification of single‐chain protease inhibitor from corn seeds. J Chromatogr 1986; 363: 315–21.3771690 [PubMed]

11 Wen L, Huang JK, Zen KC, Johnson BH, Muthukrishnan S, MacKay V, Manney TR, Manney M, Reeck GR. Nucleotide sequence of a cDNA clone that encodes the maize inhibitor of trypsin and activated Hageman factor. Plant Mol Biol 1992; 18: 813–14.1558956 [PubMed]

12 Chen Y. Distribution of Trypsin Inhibitors in Plant Food Stuffs. Food Science. Manhattan, KS: Kansas State University, 1972.

13 Hazegh‐Azam M, Kim SS, Masoud S, Andersson L, White F, Johnson L, Muthukrishnan S, Reeck G. The corn inhibitor of activated Hageman factor: purification and properties of two recombinant forms of the protein. Protein Expr Purif 1998; 13: 143–9.9675055 [PubMed]

14 Hansson KM, Nielsen S, Elg M, Deinum J. The effect of corn trypsin inhibitor and inhibiting antibodies for FXIa and FXIIa on coagulation of plasma and whole blood. J Thromb Haemost 2014; 12: 1678–86.25142753 [OpenAIRE] [PubMed]

15 Chen I, Mitchell HL. Trypsin inhibitors in plants. Phytochemistry 1973; 12: 327–30.

48 references, page 1 of 4
Abstract
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. Summary Background Corn trypsin inhibitor (CTI) has selectivity for the serine proteases coagulation factor XII and trypsin. CTI is in widespread use as a reagent that specifically inhibits the intrinsic pathway of blood coagulation but not the extrinsic pathway. Objectives To investigate the mole...
Subjects
free text keywords: Original Article, COAGULATION, Original Articles, corn trypsin inhibitor, factor XII, molecular docking simulation, serine protease, trypsin, factor XII, Hematology, Biochemistry, biology.protein, biology, Salt bridge, Serine, medicine.drug, medicine, business.industry, business, Coagulation Factor XII, Protease, medicine.medical_treatment, Docking (molecular)
Related Organizations
48 references, page 1 of 4

1 Stavrou E, Schmaier AH. Factor XII: what does it contribute to our understanding of the physiology and pathophysiology of hemostasis & thrombosis. Thromb Res 2010; 125: 210–15.20022081 [OpenAIRE] [PubMed]

2 Henriques ES, Floriano WB, Reuter N, Melo A, Brown D, Gomes JANF, Maigret B, Nascimento MAC, Ramos MJ. The search for a new model structure of b‐Factor XIIa. J Comput Aided Mol Des 2001; 15: 309–22.11349814 [PubMed]

3 Pathak M, Wilmann P, Awford J, Li C, Hamad BK, Fischer PM, Dreveny I, Dekker LV, Emsley J. Coagulation factor XII protease domain crystal structure. J Throm b Haemost 2015; 13: 580–91.25604127 [OpenAIRE] [PubMed]

4 Citarella F, Ravon DM, Pascucci B, Felici A, Fantoni A, Hack CE. Structure/function analysis of human factor XII using recombinant deletion mutants. Evidence for an additional region involved in the binding to negatively charged surfaces. Eur J Biochem 1996; 238: 240–9.8665943 [OpenAIRE] [PubMed]

5 Iwaki T, Castellino FJ. Plasma levels of bradykinin are suppressed in factor XII‐deficient mice. Thromb Haemost 2006; 95: 1003–10.16732380 [OpenAIRE] [PubMed]

6 Emsley J, McEwan PA, Gailani D. Structure and function of factor XI. Blood 2010; 115: 2569–77.20110423 [OpenAIRE] [PubMed]

7 Pauer HU, Renne T, Hemmerlein B, Legler T, Fritzlar S, Adham I, Muller‐Esterl W, Emons G, Sancken U, Engel W, Burfeind P. Targeted deletion of murine coagulation factor XII gene – a model for contact phase activation in vivo . Thromb Haemost 2004; 92: 503–8.15351846 [PubMed]

8 Renne T, Pozgajova M, Gruner S, Schuh K, Pauer HU, Burfeind P, Gailani D, Nieswandt B. Defective thrombus formation in mice lacking coagulation factor XII. J Exp Med 2005; 202: 271–81.16009717 [OpenAIRE] [PubMed]

9 Ng TB. Naturally occurring anti‐insect proteins: current status and future aspects In: Rai M, Carpinella MC, eds. Naturally Occurring Bioactive Compounds. Amsterdam: Elsevier, 2006: 409–10.

10 Lei MG, Reeck GR. Combined use of trypsin‐agarose affin ity chromatography and reversed‐phase high‐performance liquid chromatography for the purification of single‐chain protease inhibitor from corn seeds. J Chromatogr 1986; 363: 315–21.3771690 [PubMed]

11 Wen L, Huang JK, Zen KC, Johnson BH, Muthukrishnan S, MacKay V, Manney TR, Manney M, Reeck GR. Nucleotide sequence of a cDNA clone that encodes the maize inhibitor of trypsin and activated Hageman factor. Plant Mol Biol 1992; 18: 813–14.1558956 [PubMed]

12 Chen Y. Distribution of Trypsin Inhibitors in Plant Food Stuffs. Food Science. Manhattan, KS: Kansas State University, 1972.

13 Hazegh‐Azam M, Kim SS, Masoud S, Andersson L, White F, Johnson L, Muthukrishnan S, Reeck G. The corn inhibitor of activated Hageman factor: purification and properties of two recombinant forms of the protein. Protein Expr Purif 1998; 13: 143–9.9675055 [PubMed]

14 Hansson KM, Nielsen S, Elg M, Deinum J. The effect of corn trypsin inhibitor and inhibiting antibodies for FXIa and FXIIa on coagulation of plasma and whole blood. J Thromb Haemost 2014; 12: 1678–86.25142753 [OpenAIRE] [PubMed]

15 Chen I, Mitchell HL. Trypsin inhibitors in plants. Phytochemistry 1973; 12: 327–30.

48 references, page 1 of 4
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