Abstract
Reactive centre loop mutants of α-1-antitrypsin reveal position-specific effects on intermediate formation along the polymerization pathway
Highlights
The serine protease inhibitor superfamily plays important roles in controlling a wide range of proteolytic cascades [1]
Point mutations that perturb the balance between metastable and stable states result in diseases, termed serpinopathies, in which ordered polymers are retained within the endoplasmic reticulum of the cell of synthesis [3], and aggregate as inclusions associated with toxicity and cell death [4]
We determined the effect of these mutations on the rate of activation to the intermediate state by monitoring changes in tryptophan fluorescence, CD and binding to bis-8-anilinonaphthalene-1-sulfonic acid (ANS), and we report a novel FRET (Forster resonance energy transfer)-based polymerization assay
Summary
The serine protease inhibitor (serpin) superfamily plays important roles in controlling a wide range of proteolytic cascades [1]. We determined the effect of these mutations on the rate of activation to the intermediate state by monitoring changes in tryptophan fluorescence, CD and binding to bis-ANS, and we report a novel FRET (Forster resonance energy transfer)-based polymerization assay.
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