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  • Title: Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerization.
    Author: Krishnan B, Gierasch LM.
    Journal: Nat Struct Mol Biol; 2011 Feb; 18(2):222-6. PubMed ID: 21258324.
    Abstract:
    The conformational plasticity of serine protease inhibitors (serpins) underlies both their activities as protease inhibitors and their susceptibility to pathogenic misfolding and aggregation. Here, we structurally characterize a sheet-opened state of the serpin α-1 antitrypsin (α₁AT) and show how local unfolding allows functionally essential strand insertion. Mutations in α₁AT that cause polymerization-induced serpinopathies map to the labile region, suggesting that the evolution of serpin function required sampling of high risk conformations on a dynamic energy landscape.
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