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TitleThe structural basis for Z α-antitrypsin polymerization in the liver.
Journal, issue, pagesSci Adv, Vol. 6, Issue 43, Year 2020
Publish dateOct 21, 2020
AuthorsSarah 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 /
PubMed AbstractThe 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.
External linksSci Adv / PubMed:33087346 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.9 - 26.4 Å
Structure data

EMDB-4620:
A dimer component of alpha-1 antitrypsin heat-induced polymers generated from wild-type M plasma protein and decorated with Fab 4B12
Method: EM (single particle) / Resolution: 26.4 Å

EMDB-4631:
A dimer component of alpha-1 antitrypsin polymers isolated from ZZ explant liver tissue and decorated with Fab 4B12 (component B with ~90 degree rotation around the dimer axis)
Method: EM (single particle) / Resolution: 24.8 Å

EMDB-4632:
A dimer component of alpha-1 antitrypsin polymers isolated from ZZ explant liver tissue and decorated with Fab 4B12 (component A with ~60 degree rotation around the dimer axis)
Method: EM (single particle) / Resolution: 19.1 Å

PDB-6qu9:
Fab fragment of an antibody that inhibits polymerisation of alpha-1-antitrypsin
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-NA:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • Homo sapiens (human)
  • mus musculus (house mouse)
KeywordsPROTEIN BINDING / Alpha-1 antitrypsin / Z variant / polymers / protein aggregation / monoclonal antibody / Fab fragment / COPD / protease inhibitor / glycoprotein / deficiency

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