The functional domain of hirudin, a thrombin-specific inhibitor.
Hirudin is a thrombin-specific inhibitor of Mr 8000 (65 amino acid residues). Native hirudin contains 3 disulfide linkages within the first 39 amino-terminal residues, and a highly acidic C-terminal segment which is freely accessible to enzyme digestion by both endo- and exo-peptidases. Removal of the acidic C-terminal amino acids of native hirudin by both chemical and enzymatic methods resulted in a concomitant loss of hirudin inhibition activity. It is concluded that this acidic C-terminal segment of hirudin is essential for hirudin-thrombin interaction. The implication of the hirudin-thrombin interaction for the enzymatic specificity of thrombin is also discussed.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002415:Cats; D002417:Cattle; D004285:Dogs; D005344:Fibrinopeptide A / Q000032:analysis; D005345:Fibrinopeptide B / Q000032:analysis; D000882:Haplorhini; D006629:Hirudins / Q000032:analysis*; D006736:Horses; D007865:Leeches; D012756:Sheep; D013552:Swine; D013917:Thrombin / Q000037:antagonists & inhibitors
D006629:Hirudins; D005344:Fibrinopeptide A; D005345:Fibrinopeptide B; D013917:Thrombin