Probing the distance between the two binding sites of hirudin for its interaction with the active site and the fibrin(ogen)-binding site of alpha-thrombin.
The interaction of delta (Ser50)-hirudin with alpha-thrombin has been investigated. Deletion of Ser50 of r-hirudin caused a 2.7 fold increase of the Ki for its complex with alpha-thrombin. Determination of the rate constants kon and koff for complex formation showed that this effect was mainly due to a change in koff.
Wagner
U
U
Institut für Biochemie, Technische Hochschule Darmstadt.
Schmitz
T
T
Otte
M
M
Dodt
J
J
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D005337:Fibrin / Q000378:metabolism; D005340:Fibrinogen / Q000378:metabolism; D006629:Hirudins / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D009154:Mutation; D009842:Oligopeptides / Q000737:chemistry; D013917:Thrombin / Q000037:antagonists & inhibitors / Q000378:metabolism*
D006629:Hirudins; D009842:Oligopeptides; D005337:Fibrin; D005340:Fibrinogen; D013917:Thrombin