Ontology highlight
ABSTRACT:
SUBMITTER: Krishnan B
PROVIDER: S-EPMC3074950 | biostudies-literature | 2011 Feb
REPOSITORIES: biostudies-literature
Krishnan Beena B Gierasch Lila M LM
Nature structural & molecular biology 20110123 2
The conformational plasticity of serine protease inhibitors (serpins) underlies both their activities as protease inhibitors and their susceptibility to pathogenic misfolding and aggregation. Here, we structurally characterize a sheet-opened state of the serpin α-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 funct ...[more]