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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...
| Autores principales: | , |
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| Formato: | Texto |
| Lenguaje: | English |
| Publicado: |
2011
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3074950/ https://www.ncbi.nlm.nih.gov/pubmed/21258324 http://dx.doi.org/10.1038/nsmb.1976 |