Abstract:
:Six lysyl residues of human thrombin (LysB21, LysB52, LysB65, LysB106, LysB107 and LysB154) have been previously shown to participate in the binding site of hirudin, a thrombin-specific inhibitor [(1989) J. Biol. Chem. 264, 7141-7146]. In this report, we attempted to delineate the region of hirudin which binds to these basic amino acids of thrombin. Using the N-terminal core domains (r-Hir1-43 and r-Hir1-52) derived from recombinant hirudins and synthetic C-terminal peptides (Hir40-65 and Hir52-65)--all fragments form complexes with thrombin--we are able to demonstrate that the structural elements of hirudin which account for the shielding of these 6 lysyl residues are exclusively located within the acidic C-terminal region. Since hirudin C-terminal peptides were shown to bind to a non-catalytic site of thrombin and inhibit its interaction with fibrinogen [(1987) FEBS Lett. 211, 10-16], our data consequently imply that these 6 lysyl residues are constituents of the fibrinogen recognition site of thrombin.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Chang JY,Ngai PK,Rink H,Dennis S,Schlaeppi JMdoi
10.1016/0014-5793(90)80573-2subject
Has Abstractpub_date
1990-02-26 00:00:00pages
287-90issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(90)80573-2journal_volume
261pub_type
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