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Nature 444, 153-155 (9 November 2006) | doi:10.1038/nature05305; Published online 11 October 2006

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Structural biology: Enzyme theory holds water

Matthew Freeman1

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Intramembrane proteases have attracted much attention because of their biological and medical value. The first crystal structure of one of these enzymes begins to solve the mystery of how they work.

Proteases are some of the most potent tools to which a cell has access, because, unlike most other protein-modifying enzymes, they catalyse an essentially irreversible reaction — the breaking of peptide bonds. This can obviously be used to degrade unwanted proteins, but proteases also have many vital regulatory functions1.

  1. Matthew Freeman is at the MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
    Email: mf1@mrc-lmb.cam.ac.uk

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