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

abstract

• 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 Å 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 α-thrombin that may modulate the physiological activity of thrombin. Copyright © 2007 American Chemical Society.

authors

• Liu, Wenshe

author list (cited authors)

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

complete list of authors

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

publication date

• January 1, 2010 11:11 AM

publisher

• American Chemical Society (ACS)  Publisher

published in

• Journal of the American Chemical Society  Journal

keywords

• Crystallography, X-Ray
• Hirudins
• Models, Molecular
• Protein Conformation
• Thrombin
• Tyrosine

PubMed Central ID

• 17685615

Digital Object Identifier (DOI)

• 10.1021/ja0735002

start page

• 10648

end page

• 10649

volume

• 129

issue

• 35