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Antithrombin Rouen‐IV 24 Arg→Cys The amino‐terminal contribution to heparin binding
Author(s) -
Borg J.-Y.,
Brennan S.O.,
Carrell R.W.,
George P.,
Perry D.J.,
Shaw J.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81530-2
Subject(s) - antithrombin , heparin , arginine , amino terminal , chemistry , cysteine , biochemistry , protease , binding site , microbiology and biotechnology , peptide sequence , amino acid , biology , enzyme , gene
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 Å 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.