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Serpin metastability and protease inhibition

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The family of serine protease inhibitors known as the serpins is represented in all branches of life. They have evolved an extraordinary mechanism to inhibit proteases that distinguishes them from the 20 other families of serine protease inhibitors, and renders them uniquely qualified to control of the proteolytic pathways essential to life. The mechanism resembles the grizzly action of a spring-loaded mousetrap, where the protease is the mouse and the serpin is a set and baited trap. When the protease nibbles the bait, the trap is sprung, crushing the unsuspecting protease. As with a mousetrap, the active state of a serpin is metastable, and the energy released upon conversion to its more stable form is used to crush the protease. By solving crystallographic structures of serpins in various forms, we have developed a frame-by-frame cinematic view of this remarkable mechanism.

This talk is part of the Physics of Medicine Roadshow series.

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