Title : Degeneracy of the Antithrombin Binding Sequence in Heparin: 2-O-Sulfated Iduronic Acid Can Replace the Critical Glucuronic Acid.

Pub. Date : 2020 Sep 10

PMID : 32515841






4 Functional Relationships(s)
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1 Degeneracy of the antithrombin binding sequence in heparin: 2-O-sulfated Iduronic acid can replace the critical glucuronic acid. Glucuronic Acid serpin family C member 1 Homo sapiens
2 Heparin binds to and activates antithrombin (AT) through a specific pentasaccharide sequence in which a trisaccharide subsite, containing glucuronic acid (GlcA), has been considered as the initiator in the recognition of the polysaccharide by the protein. Glucuronic Acid serpin family C member 1 Homo sapiens
3 Heparin binds to and activates antithrombin (AT) through a specific pentasaccharide sequence in which a trisaccharide subsite, containing glucuronic acid (GlcA), has been considered as the initiator in the recognition of the polysaccharide by the protein. Glucuronic Acid serpin family C member 1 Homo sapiens
4 Indeed, a heparin octasaccharidic sequence obtained by chemoenzymatic synthesis, in which GlcA is replaced by IdoA2S has been found to similarly bind to and activate antithrombin. Glucuronic Acid serpin family C member 1 Homo sapiens