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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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| Main Authors: | , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2011
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| 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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