The structural basis for Z α₁-antitrypsin polymerization in the liver.

ABSTRACT: The serpinopathies are among a diverse set of conformational diseases that involve the aberrant self-association of proteins into ordered aggregates. α₁-Antitrypsin deficiency is the archetypal serpinopathy and results from the formation and deposition of mutant forms of α₁-antitrypsin as "polymer" chains in liver tissue. No detailed structural analysis has been performed of this material. Moreover, there is little information on the relevance of well-studied artificially induced polymers to these disease-associated molecules. We have isolated polymers from the liver tissue of Z α₁-antitrypsin homozygotes (E342K) who have undergone transplantation, labeled them using a Fab fragment, and performed single-particle analysis of negative-stain electron micrograp

SUBMITTER: Faull SV 

PROVIDER: S-EPMC7577719 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature