Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerization
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology
Link
http://www.nature.com/articles/nsmb.1976.pdf
Reference37 articles.
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2. Huntington, J.A., Read, R.J. & Carrell, R.W. Structure of a serpin-protease complex shows inhibition by deformation. Nature 407, 923–926 (2000).
3. Dupont, D.M. et al. Biochemical properties of plasminogen activator inhibitor-1. Front. Biosci. 14, 1337–1361 (2009).
4. Mushunje, A., Evans, G., Brennan, S.O., Carrell, R.W. & Zhou, A. Latent antithrombin and its detection, formation and turnover in the circulation. J. Thromb. Haemost. 2, 2170–2177 (2004).
5. Kaslik, G. et al. Effects of serpin binding on the target proteinase: global stabilization, localized increased structural flexibility, and conserved hydrogen bonding at the active site. Biochemistry 36, 5455–5464 (1997).
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