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Dynamic local unfolding in the serpinalpha-1 antitrypsin provides a mechanism for loop insertion and polymerization

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 (α(1)AT) and show how local unfolding allows functionally essen...

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Detalhes bibliográficos
Main Authors: Krishnan, Beena, Gierasch, Lila M.
Formato: Artigo
Idioma:Inglês
Publicado em: 2011
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC3074950/
https://ncbi.nlm.nih.gov/pubmed/21258324
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/nsmb.1976
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