Title : The signature 3-O-sulfo group of the anticoagulant heparin sequence is critical for heparin binding to antithrombin but is not required for allosteric activation.

Pub. Date : 2009 Oct 2

PMID : 19661062






3 Functional Relationships(s)
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1 By contrast, mutation of Lys(114) solely affected the preferential interaction of the pentasaccharide with activated antithrombin. Lysine serpin family C member 1 Homo sapiens
2 These findings demonstrate that the 3-O-sulfo group functions as a key determinant of heparin pentasaccharide activation of antithrombin both by contributing to the Lys(114)-independent recognition of native antithrombin and by triggering a Lys(114)-dependent induced fit interaction with activated antithrombin that locks the serpin in the activated state. Lysine serpin family C member 1 Homo sapiens
3 These findings demonstrate that the 3-O-sulfo group functions as a key determinant of heparin pentasaccharide activation of antithrombin both by contributing to the Lys(114)-independent recognition of native antithrombin and by triggering a Lys(114)-dependent induced fit interaction with activated antithrombin that locks the serpin in the activated state. Lysine serpin family C member 1 Homo sapiens