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 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.

authors

• Liu, Wenshe

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

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

URL

• http%3A%2F%2Fdx.doi.org%2F10.1021%2Fja0735002