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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Mutations on the hinge region of leukocyte elastase inhibitor determine the loss of inhibitory function.

Leukocyte elastase inhibitor (LEI) is a cytosolic component of lung macrophages and blood leukocytes that inhibits neutrophil elastase. LEI is a member of the serpin superfamily, these proteins, mostly protease inhibitors, are thought to undergo a conformational change upon complex formation with proteinase that involves partial insertion of the hinge region of the reactive centre loop into a beta-sheet of the inhibitor. In this work three mutations were produced in the hinge region of elastase inhibitor that abolish the inhibition activity of LEI and transform the protein in a substrate of the elastase. This result demonstrates that the inhibitory mechanism of serpin is common to LEI.[1]

References

  1. Mutations on the hinge region of leukocyte elastase inhibitor determine the loss of inhibitory function. Perani, P., Zeggai, S., Torriglia, A., Courtois, Y. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
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