By James Travis (auth.), Frank C. Church, Dennis D. Cunningham, David Ginsburg, Maureane Hoffman, Stuart R. Stone, Douglas M. Tollefsen (eds.)

`The editors have succeeded in generating a quantity of labor which gives many solutions to questions, requested and unasked, a few seriously vital box of biologic learn. it's going to be within the library of any scientist with an curiosity in human body structure; it might be helpful to many different researchers as well.'
Chemtracts - Biochemistry and Molecular Biology, 12:10 (1999)

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4 x 10-3 M, is converted by a conformational change to a stable complex at a rate constant of -10 S-I 33. This conformational change is reflected in altered antigenic, spectroscopic and heparinbinding properties of antithrombin 37,39--41. The inactivation of a target proteinase by antithrombin is initiated by the enzyme recognizing the reactive bond of the inhibitor42-44. The PI residue of this bond, Arg-393, is essential for the recognition, as shown by congenital antithrombin variants with mutations of this residue being inactive45-47.

A. (1994) Site-directed mutagenesis of the P2 residue of human antithrombin. FEBS Lett. 339: 147-150. 53. P. A. (1994) Amino acid substitutions of the P2 residue of human antithrombin that either enhance or impair function. Thromb. Res. 75: 293-305. 54. , Lawrence, DA, Ginsburg, D. and Bjork, I. (1995) Role of the catalytic serine in the interactions of serine proteinases with protein inhibitors of the serpin familyContribution of a covalent interaction to the binding energy of serpin-proteinase complexes.

E. (1991) Mobile reactive centre of serpins and the control of thrombosis. Nature 353: 576-578. 31. , Olson, S. T. E. (1992) Conversion of antithrombin from an inhibitor of thrombin to a substrate with reduced heparin affinity and enhanced conformational stability by binding ofa tetradecapeptide corresponding to the PI to PI4 region of the putative reactive bond loop of the inhibitor. J. BioI. Chern. 267: 1976-1982. 32. A. and Huber, R. (1992) Evidence for the extent of insertion of the active site loop of intact a l proteinase inhibitor in ~-sheet A.

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