Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerization.
Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerization.
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DOI：
10.1038/nsmb.1976
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发表时间：
2011-02
影响因子：
16.8
通讯作者：
中科院分区：
文献类型：
--
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The conformational plasticity of serpins underlies both their activities as protease inhibitors and their susceptibility to pathogenic misfolding. Here, we structurally characterize a sheet-opened state of the serpin alpha-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 them to sample conformations on a dynamic energy landscape that increased risk of aggregation.
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影响因子：
5.6
作者：
Tew, DJ;Bottomley, SP
通讯作者：
Bottomley, SP
影响因子：
6
作者：
Mahadeva, R;Atkinson, C;Lomas, DA
通讯作者：
Lomas, DA
DOI：
10.1073/pnas.1004785107
发表时间：
2010-10-05
影响因子：
11.1
作者：
Ekeowa, Ugo I.;Freeke, Joanna;Lomas, David A.
通讯作者：
Lomas, David A.
影响因子：
5.6
作者：
Knaupp, Anja S.;Levina, Vita;Bottomley, Stephen P.
通讯作者：
Bottomley, Stephen P.
影响因子：
10.4
作者：
Mushunje, A;Evans, G;Zhou, A
通讯作者：
Zhou, A