A novel DFP tripeptide motif interacts with the coagulation factor XI apple 2 domain

Author:

Wong Szu S.12,Østergaard Søren2,Hall Gareth1,Li Chan1,Williams Philip M.1,Stennicke Henning2,Emsley Jonas1ORCID

Affiliation:

1. Centre for Biomolecular Sciences, School of Pharmacy, University of Nottingham, Nottingham, United Kingdom; and

2. Novo Nordisk, Måløv, Denmark

Abstract

Key Points A novel FXI binding tripeptide motif has sequence Asp-Phe-Pro (DFP). FXI complex crystal structures reveal DFP peptides bound to the apple 2 domain.

Publisher

American Society of Hematology

Subject

Cell Biology,Hematology,Immunology,Biochemistry

Reference45 articles.

1. Factor XI and contact activation as targets for antithrombotic therapy.;Gailani;J Thromb Haemost,2015

2. Human blood coagulation factor XI. Purification, properties, and mechanism of activation by activated factor XII.;Bouma;J Biol Chem,1977

3. Amino acid sequence of human factor XI, a blood coagulation factor with four tandem repeats that are highly homologous with plasma prekallikrein.;Fujikawa;Biochemistry,1986

4. Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains.;McMullen;Biochemistry,1991

5. Crystal structure of the factor XI zymogen reveals a pathway for transactivation.;Papagrigoriou;Nat Struct Mol Biol,2006

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