A novel pathological mutant reveals the role of torsional flexibility in the serpin breach in adoption of an aggregation‐prone intermediate
Kamila Kamuda,
Riccardo Ronzoni,
Avik Majumdar
et al.
Abstract:Mutants of alpha‐1‐antitrypsin cause the protein to self‐associate and form ordered aggregates (‘polymers’) that are retained within hepatocytes, resulting in a predisposition to the development of liver disease. The associated reduction in secretion, and for some mutants, impairment of function, leads to a failure to protect lung tissue against proteases released during the inflammatory response and an increased risk of emphysema. We report here a novel deficiency mutation (Gly192Cys), that we name the Sydney… Show more
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