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Free Content The serpins: nature's molecular Mousetraps

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A special family of inhibitors, known as the serpins, has evolved an extraordinary mechanism to enable the control of the proteolytic pathways essential to life. The serpins undergo a profound change in conformation to entrap their target protease in an irreversible complex. The solving of the structure of this complex now completes a video depiction of the changes involved. The serpin, just like a mousetrap, is seen to change with a spring-like movement from an initial metastable state to a final hyperstable form. The structure shows how this conformational shift not only inhibits the protease but also destroys it. A bonus from these structural insights is the realisation that a number of diseases, as diverse as thrombosis, cirrhosis and dementia, all share a common mechanism arising from similar mutations of different serpins.
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Document Type: Research Article

Affiliations: University of Cambridge, Department of Haematology, Wellcome Trust Centre for Molecular Mechanisms in Disease, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 2XY, UK

Publication date: 2001-05-15

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