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Switching serine protease specificity

Nature Structural Biology volume 5, pages 933–937 (1998)Cite this article

Abstract

The modulation of enzymatic activity by a protein cofactor may be accomplished in several ways, as illustrated by two new structures.

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Figure 1: Ribbon diagrams of the staphylokinase–microplasmin (SAK-μPL) structure (left) and the streptokinase–microplasmin (SK-μPL) structure (right).
Figure 2: Rotated ribbon diagrams of SK–μPL and SAK–μPL complexes.
Figure 3: Differential effects of α2-plasmin inhib- itor on the streptokinase–plasmin and staphylokinase–plasmin complexes.
Figure 4: A simplified blood coagulation cascade.

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Authors and Affiliations

  1. Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, University of Oklahoma Health Sciences Center, and the Howard Hughes Medical Institute, Oklahoma City, 73104, Oklahoma, USA

    Charles T. Esmon & Timothy Mather

  2. Departments of Pathology, Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, and the Howard Hughes Medical Institute, Oklahoma City, 73104, Oklahoma, USA

    Charles T. Esmon

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  1. Charles T. Esmon
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Correspondence to Charles T. Esmon.

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Esmon, C., Mather, T. Switching serine protease specificity. Nat Struct Mol Biol 5, 933–937 (1998). https://doi.org/10.1038/2906

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