The structural basis for Z α 1 -antitrypsin polymerization in the liver

Author:

Faull Sarah V.1ORCID,Elliston Emma L. K.12ORCID,Gooptu Bibek345ORCID,Jagger Alistair M.12ORCID,Aldobiyan Ibrahim12,Redzej Adam5ORCID,Badaoui Magd1ORCID,Heyer-Chauhan Nina12ORCID,Rashid S. Tamir6ORCID,Reynolds Gary M.7ORCID,Adams David H.7ORCID,Miranda Elena8,Orlova Elena V.5ORCID,Irving James A.12ORCID,Lomas David A.12ORCID

Affiliation:

1. UCL Respiratory, University College London, 5 University Street, London WC1E 6JF, UK.

2. Institute of Structural and Molecular Biology, University College London, Gower Street, London WC1E 6BN, UK.

3. Leicester Institute of Structural and Chemical Biology, University of Leicester, Henry Wellcome Building, Lancaster Road, Leicester LE1 7HB, UK.

4. National Institute for Health Research (NIHR) Leicester BRC-Respiratory, Leicester, UK.

5. Institute of Structural and Molecular Biology, Birkbeck College, Malet Street, University of London, London WC1E 7HX, UK.

6. Centre for Stem Cells and Regenerative Medicine and Institute for Liver Studies, King’s College London, London WC2R 2LS, UK.

7. Centre for Liver Research and NIHR Birmingham Liver Biomedical Research Unit, Institute of Immunology and Immunotherapy, University of Birmingham, Birmingham, UK.

8. Department of Biology and Biotechnologies “Charles Darwin” and Pasteur Institute—Cenci Bolognetti Foundation, Sapienza University of Rome, Rome, Italy.

Abstract

α 1 -Antitrypsin polymers from human tissue have a structure most consistent with an intermolecular C-terminal domain swap.

Funder

Alpha-1 Foundation

Wellcome

Medical Research Council

Engineering and Physical Sciences Research Council

NIHR UCLH Biomedical research centre

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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