-
Antithrombin Rouen-IV 24 Arg----Cys. The amino-terminal contribution to heparin binding.
Laboratoire d'hemostase, Centre Hospitalier Universitaire, Rouen, France.
A variant antithrombin with reduced heparin affinity was shown by mass spectrometry sequencing and DNA amplification to have a substitution of a cysteine for an arginine at residue 24. The position of Arg-24 can be fixed within a 12 A radius from the bridge at Cys-21. This is compatible with findings in the homologous protease nexin-1 which indicate an extension of the binding site of heparin from the D-helix to under the adjacent amino-terminal pole.
PMID: 2365065 [PubMed - indexed for MEDLINE]
-
Cited by 3 PubMed Central articles
-
The N-terminal segment of antithrombin acts as a steric gate for the binding of heparin.
Fitton HL, Skinner R, Dafforn TR, Jin L, Pike RN.
Protein Sci. 1998 Mar; 7(3):782-8.
[Protein Sci. 1998]
-
ReviewGlycosaminoglycans and the regulation of blood coagulation.
Bourin MC, Lindahl U.
Biochem J. 1993 Jan 15; 289 ( Pt 2):313-30.
[Biochem J. 1993]
-
Pleiotropic effects of antithrombin strand 1C substitution mutations.
Lane DA, Olds RJ, Conard J, Boisclair M, Bock SC, Hultin M, Abildgaard U, Ireland H, Thompson E, Sas G.
J Clin Invest. 1992 Dec; 90(6):2422-33.
[J Clin Invest. 1992]