Add time:07/22/2019         Source:sciencedirect.com

Publisher SummaryThis chapter describes the hirudin and hirudin-based peptides. Hirudin and hirudin-based peptides have served as exemplary tools for the studies on thrombin structure-function relationships and on thrombin biological activities. Binding of hirudin and peptide fragments with thrombin serves as a model for protein-protein and, in particular, protease-inhibitor interactions. In natural hirudin isolated from the leech, Tyr-63’ is sulfated, which further increases the number of negatively charged residues in this region. This post-translational modification is not, however, found in recombinant molecules expressed in Escherichia coli or yeast. The structure of the thrombin-hirudin complex discussed in the chapter shows the novel mechanism by which hirudin inhibits thrombin. The N-terminal three residues of hirudin are bound in the active site cleft of thrombin, but the orientation of the polypeptide chain is opposite to that observed for other protein inhibitors of serine proteinases. The remainder of the N-terminal core region of hirudin closes off the active site of thrombin. The C-terminal tail of hirudin extends 35 Ǻ across the surface of thrombin and is bound to a surface groove (the anion-binding exosite) that is rich in basic amino acids.

We also recommend Trading Suppliers and Manufacturers of HIRUDIN (54-65) (SULFATED) (cas 109528-49-6). Pls Click Website Link as below: cas 109528-49-6 suppliers