Antithrombin Rouen-IV 24 Arg----Cys. The amino-terminal contribution to heparin binding

FEBS Lett. 1990 Jun 18;266(1-2):163-6. doi: 10.1016/0014-5793(90)81530-2.

Abstract

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.

Publication types

  • Case Reports
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Antithrombin Proteins
  • Antithrombins / genetics
  • Antithrombins / metabolism*
  • Base Sequence
  • Binding Sites
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism
  • Heparin / metabolism*
  • Humans
  • Male
  • Molecular Sequence Data
  • Oligonucleotide Probes
  • Protein Conformation
  • Structure-Activity Relationship

Substances

  • Antithrombin Proteins
  • Antithrombins
  • Carrier Proteins
  • Oligonucleotide Probes
  • antithrombin Rouen IV
  • Heparin