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Cleaved antitrypsin polymers at atomic resolution

  • MICHELLE A. DUNSTONE (a1), WEIWEN DAI (a2), JAMES C. WHISSTOCK (a2), JAMIE ROSSJOHN (a1), ROBERT N. PIKE (a2), SUSANNE C. FEIL (a1), BERNARD F. LE BONNIEC (a3), MICHAEL W. PARKER (a1) and STEPHEN P. BOTTOMLEY (a2)...

Abstract

α1-Antitrypsin deficiency, which can lead to both emphysema and liver disease, is a result of the accumulation of α1-antitrypsin polymers within the hepatocyte. A wealth of biochemical and biophysical data suggests that α1-antitrypsin polymers form via insertion of residues from the reactive center loop of one molecule into the β-sheet of another. However, this long-standing hypothesis has not been confirmed by direct structural evidence. Here, we describe the first crystallographic evidence of a β-strand linked polymer form of α1-antitrypsin: the crystal structure of a cleaved α1-antitrypsin polymer.

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Corresponding author

Reprint requests to: Stephen P. Bottomley, The Department of Biochemistry and Molecular Biology, Monash University, Clayton Campus, Melbourne, Victoria, 3168 Australia; e-mail: Steve.Bottomley@med.monash.edu.au.

Keywords

Cleaved antitrypsin polymers at atomic resolution

  • MICHELLE A. DUNSTONE (a1), WEIWEN DAI (a2), JAMES C. WHISSTOCK (a2), JAMIE ROSSJOHN (a1), ROBERT N. PIKE (a2), SUSANNE C. FEIL (a1), BERNARD F. LE BONNIEC (a3), MICHAEL W. PARKER (a1) and STEPHEN P. BOTTOMLEY (a2)...

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