2pw8
From Proteopedia
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Crystal structure of sulfo-hirudin complexed to thrombin
Overview
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 A 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 alpha-thrombin that may modulate the, physiological activity of thrombin.
About this Structure
2PW8 is a Protein complex structure of sequences from Hirudo medicinalis and Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal Structure of a Biosynthetic Sulfo-hirudin Complexed to Thrombin., Liu CC, Brustad E, Liu W, Schultz PG, J Am Chem Soc. 2007 Aug 9;. PMID:17685615
Page seeded by OCA on Wed Jan 23 12:33:46 2008
Categories: Hirudo medicinalis | Homo sapiens | Protein complex | Brustad, E. | Liu, C.C. | Liu, W. | Schultz, P.G. | NA | NI | Hirudin | Hydrolase | Sulfotyrosine | Thrombin
