Crystal structure of a biosynthetic sulfo-hirudin complexed to thrombin.
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abstract
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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.
author list (cited authors)
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Liu, C. C., Brustad, E., Liu, W., & Schultz, P. G
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Liu, Chang C||Brustad, Eric||Liu, Wenshe||Schultz, Peter G
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Crystallography, X-Ray
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Hirudins
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Models, Molecular
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Protein Conformation
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Thrombin
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Tyrosine
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