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• W2021567885 startingPage "e54766" @default.
• W2021567885 abstract "α(1)-Antitrypsin, the archetypal member of the serpin superfamily, is a metastable protein prone to polymerization when exposed to stressors such as elevated temperature, low denaturant concentrations or through the presence of deleterious mutations which, in a physiological context, are often associated with disease. Experimental evidence suggests that α(1)-Antitrypsin can polymerize via several alternative mechanisms in vitro. In these polymerization mechanisms different parts of the molecule are proposed to undergo conformational change. Both strand 5 and helix I are proposed to adopt different conformations when forming the various polymers, and possess a number of highly conserved residues however their role in the folding and misfolding of α(1)-Antitrypsin has never been examined. We have therefore created a range of α(1)Antitypsin variants in order to explore the role of these conserved residues in serpin folding, misfolding, stability and function. Our data suggest that key residues in helix I mediate efficient folding from the folding intermediate and residues in strand 5A ensure native state stability in order to prevent misfolding. Additionally, our data indicate that helix I is involved in the inhibitory process and that both structural elements undergo differing conformational rearrangements during unfolding and misfolding. These findings suggest that the ability of α(1)-Antitrypsin to adopt different types of polymers under different denaturing conditions may be due to subtle conformational differences in the transiently populated structures adopted prior to the I and M* states." @default.
• W2021567885 created "2016-06-24" @default.
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• W2021567885 date "2013-01-29" @default.
• W2021567885 modified "2023-09-23" @default.
• W2021567885 title "The Roles of Helix I and Strand 5A in the Folding, Function and Misfolding of α1-Antitrypsin" @default.
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• W2021567885 doi "https://doi.org/10.1371/journal.pone.0054766" @default.
• W2021567885 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3558512" @default.
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• W2021567885 hasPublicationYear "2013" @default.
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