Journal: Sci Adv / Year: 2020 Title: The structural basis for Z α-antitrypsin polymerization in the liver. Authors: Sarah V Faull / Emma L K Elliston / Bibek Gooptu / Alistair M Jagger / Ibrahim Aldobiyan / Adam Redzej / Magd Badaoui / Nina Heyer-Chauhan / S Tamir Rashid / Gary M Reynolds / David H Adams ...Authors: Sarah V Faull / Emma L K Elliston / Bibek Gooptu / Alistair M Jagger / Ibrahim Aldobiyan / Adam Redzej / Magd Badaoui / Nina Heyer-Chauhan / S Tamir Rashid / Gary M Reynolds / David H Adams / Elena Miranda / Elena V Orlova / James A Irving / David A Lomas / Abstract: The serpinopathies are among a diverse set of conformational diseases that involve the aberrant self-association of proteins into ordered aggregates. α-Antitrypsin deficiency is the archetypal ...The serpinopathies are among a diverse set of conformational diseases that involve the aberrant self-association of proteins into ordered aggregates. α-Antitrypsin deficiency is the archetypal serpinopathy and results from the formation and deposition of mutant forms of α-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 α-antitrypsin homozygotes (E342K) who have undergone transplantation, labeled them using a Fab fragment, and performed single-particle analysis of negative-stain electron micrographs. The data show structural equivalence between heat-induced and ex vivo polymers and that the intersubunit linkage is best explained by a carboxyl-terminal domain swap between molecules of α-antitrypsin.
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