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Structure-activity relationships of recombinant hirudins.
Semin Thromb Hemost. 1991 Apr; 17(2):94-8.ST

Abstract

The complex formation between thrombin and hirudin is unique among other serine proteinase-inhibitor complexes. The serpines occupy the specificity pocket of the active site of the target enzyme with an amino acid residue corresponding to the specificity of the enzyme at the P1 site of the substrate. In contrast, the Thr2 residue of hirudin approaches only the entrance of the pocket. The peptide chain of the inhibitors D-Phe-Pro-ArgCH2Cl and NAPAP is antiparallel to the enzyme backbone, whereas the N-terminal amino acids of hirudin run parallel. These unexpected interactions seem to contribute to a greater extent to the tight binding than the ionic interactions of the hirudin tail with the fibrinogen binding site of thrombin. Obviously, these interactions account for the unique selectivity of hirudin for thrombin.

Authors+Show Affiliations

Institute of Pharmacology and Toxicology, Medical Academy Erfurt, Germany.No affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Review

Language

eng

PubMed ID

1771418

Citation

Stürzebecher, J, and P Walsmann. "Structure-activity Relationships of Recombinant Hirudins." Seminars in Thrombosis and Hemostasis, vol. 17, no. 2, 1991, pp. 94-8.
Stürzebecher J, Walsmann P. Structure-activity relationships of recombinant hirudins. Semin Thromb Hemost. 1991;17(2):94-8.
Stürzebecher, J., & Walsmann, P. (1991). Structure-activity relationships of recombinant hirudins. Seminars in Thrombosis and Hemostasis, 17(2), 94-8.
Stürzebecher J, Walsmann P. Structure-activity Relationships of Recombinant Hirudins. Semin Thromb Hemost. 1991;17(2):94-8. PubMed PMID: 1771418.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structure-activity relationships of recombinant hirudins. AU - Stürzebecher,J, AU - Walsmann,P, PY - 1991/4/1/pubmed PY - 1991/4/1/medline PY - 1991/4/1/entrez SP - 94 EP - 8 JF - Seminars in thrombosis and hemostasis JO - Semin Thromb Hemost VL - 17 IS - 2 N2 - The complex formation between thrombin and hirudin is unique among other serine proteinase-inhibitor complexes. The serpines occupy the specificity pocket of the active site of the target enzyme with an amino acid residue corresponding to the specificity of the enzyme at the P1 site of the substrate. In contrast, the Thr2 residue of hirudin approaches only the entrance of the pocket. The peptide chain of the inhibitors D-Phe-Pro-ArgCH2Cl and NAPAP is antiparallel to the enzyme backbone, whereas the N-terminal amino acids of hirudin run parallel. These unexpected interactions seem to contribute to a greater extent to the tight binding than the ionic interactions of the hirudin tail with the fibrinogen binding site of thrombin. Obviously, these interactions account for the unique selectivity of hirudin for thrombin. SN - 0094-6176 UR - https://www.unboundmedicine.com/medline/citation/1771418/Structure_activity_relationships_of_recombinant_hirudins_ L2 - http://www.thieme-connect.com/DOI/DOI?10.1055/s-2007-1002595 DB - PRIME DP - Unbound Medicine ER -