Title : Heparin cofactor II is regulated allosterically and not primarily by template effects. Studies with mutant thrombins and glycosaminoglycans.

Pub. Date : 1994 Dec 30

PMID : 7806495






5 Functional Relationships(s)
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1 Thrombin is inhibited by the serpins antithrombin and heparin cofactor II (HCiI) in reactions that are accelerated markedly by specific glycosaminoglycans. Glycosaminoglycans coagulation factor II, thrombin Homo sapiens
2 The present study examines the role of anion-binding exosite II of thrombin in the interaction with glycosaminoglycans and HCII. Glycosaminoglycans coagulation factor II, thrombin Homo sapiens
3 Acceleration of thrombin inhibition by serpins in the presence of glycosaminoglycans is proposed to occur by a template mechanism, in which inhibitor and protease bind simultaneously to the same glycosaminoglycan chain, facilitating their interaction. Glycosaminoglycans coagulation factor II, thrombin Homo sapiens
4 Acceleration of thrombin inhibition by serpins in the presence of glycosaminoglycans is proposed to occur by a template mechanism, in which inhibitor and protease bind simultaneously to the same glycosaminoglycan chain, facilitating their interaction. Glycosaminoglycans coagulation factor II, thrombin Homo sapiens
5 Specific mutations in exosite II (R89E, R245E, K248E, and K252E) disrupted thrombin binding to both dermatan sulfate and heparin, indicating that both glycosaminoglycans bind to a common site in exosite II. Glycosaminoglycans coagulation factor II, thrombin Homo sapiens