Antithrombin Rouen-IV 24 Arg----Cys. The amino-terminal contribution to heparin binding.
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.
Borg
J Y
JY
Laboratoire d'hemostase, Centre Hospitalier Universitaire, Rouen, France.
Brennan
S O
SO
Carrell
R W
RW
George
P
P
Perry
D J
DJ
Shaw
J
J
D000328:Adult; D058833:Antithrombin Proteins; D000991:Antithrombins / Q000235:genetics / Q000378:metabolism*; D001483:Base Sequence; D001665:Binding Sites; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism; D006493:Heparin / Q000378:metabolism*; D006801:Humans; D008297:Male; D008969:Molecular Sequence Data; D015345:Oligonucleotide Probes; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D058833:Antithrombin Proteins; D000991:Antithrombins; D002352:Carrier Proteins; D015345:Oligonucleotide Probes; C064888:antithrombin Rouen IV; D006493:Heparin