Chargement en cours...
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...
Enregistré dans:
| Auteurs principaux: | , |
|---|---|
| Format: | Artigo |
| Langue: | Inglês |
| Publié: |
2011
|
| Sujets: | |
| Accès en ligne: | 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 |
| Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|