Title : Important role of arginine 129 in heparin-binding site of antithrombin III. Identification of a novel mutation arginine 129 to glutamine.

Pub. Date : 1990 Nov 5

PMID : 2229057






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 This amino acid is part of the ATIII region comprising residues 114-154, which contains the highest proportion of basic residues (Arg or Lys), and is known from chemical modification studies to be involved in heparin binding. Lysine serpin family C member 1 Homo sapiens
2 We propose that a cooperation between Lys-125, Arg-129, Lys-136, and Arg-47 exposed at the surface of the inhibitor allows the binding of the essential pentasaccharide domain of heparin which is specific for the ATIII interaction. Lysine serpin family C member 1 Homo sapiens
3 We propose that a cooperation between Lys-125, Arg-129, Lys-136, and Arg-47 exposed at the surface of the inhibitor allows the binding of the essential pentasaccharide domain of heparin which is specific for the ATIII interaction. Lysine serpin family C member 1 Homo sapiens