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

@article{Wong2016AND,
  title={A novel DFP tripeptide motif interacts with the coagulation factor XI apple 2 domain.},
  author={Szu S Wong and S{\o}ren {\O}stergaard and Gareth W. Hall and Chan Li and Philip M. Williams and Henning Ralf Stennicke and Jonas Emsley},
  journal={Blood},
  year={2016},
  volume={127 23},
  pages={
          2915-23
        }
}
Factor XI (FXI) is the zymogen of FXIa, which cleaves FIX in the intrinsic pathway of coagulation. FXI is known to exist as a dimer and interacts with multiple proteins via its 4 apple domains in the "saucer section" of the enzyme; however, to date, no complex crystal structure has been described. To investigate protein interactions of FXI, a large random peptide library consisting of 10(6) to 10(7) peptides was screened for FXI binding, which identified a series of FXI binding motifs… CONTINUE READING

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inventor; Novo Nordisk, assignee. Factor XI-binding proteins. World Intellectual 2922 WONG et al BLOOD, 9 JUNE 2016 x VOLUME

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