Article
Conformational changes in serpins: II. The mechanism of activation of antithrombin by heparin.
Journal of molecular biology - 1 Sept 2000
Whisstock J C, Pike R N, Jin L, Skinner R, Pei X Y, Carrell R W, Lesk A M
Abstract excerpt
Antithrombin, uniquely among plasma serpins acting as proteinase inhibitors in the control of the blood coagulation cascade, circulates in a relatively inactive form. Its activation by heparin, and specifically by a pentasaccharide core of heparin, has been shown to involve release of the peptide loop containing the reactive centre from partial insertion in the A sheet of the molecule. Here we compare the...
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