Crystal structure of a biosynthetic sulfo-hirudin complexed to thrombin. Academic Article uri icon


  • The leech-derived anticoagulant hirudin is post-translationally sulfated on tyrosine 63, resulting in a >10-fold increase in its affinity for thrombin. We report the structure of a biosynthetic sulfo-hirudin complexed to thrombin solved to 1.84 resolution and show that sulfation is responsible for a salt bridge and an extended hydrogen-bond network that taken together account for the increased affinity of sulfo-hirudin for thrombin. We also identify a divalent cation binding site at the interface between the two subunits of -thrombin that may modulate the physiological activity of thrombin. Copyright 2007 American Chemical Society.

published proceedings

  • J Am Chem Soc

altmetric score

  • 3

author list (cited authors)

  • Liu, C. C., Brustad, E., Liu, W., & Schultz, P. G.

citation count

  • 54

complete list of authors

  • Liu, Chang C||Brustad, Eric||Liu, Wenshe||Schultz, Peter G

publication date

  • September 2007