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Protein Science, Vol 9, Issue 2 417-420, Copyright © 2000 by The Protein Society

JOURNAL ARTICLE

Cleaved antitrypsin polymers at atomic resolution

MA Dunstone, W Dai, JC Whisstock, J Rossjohn, RN Pike, SC Feil, BF Le Bonniec, MW Parker and SP Bottomley
The Ian Potter Foundation Protein Crystallography Laboratory, St Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.

Alpha1-antitrypsin deficiency, which can lead to both emphysema and liver disease, is a result of the accumulation of alpha1-antitrypsin polymers within the hepatocyte. A wealth of biochemical and biophysical data suggests that alpha1-antitrypsin polymers form via insertion of residues from the reactive center loop of one molecule into the beta- 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 beta-strand linked polymer form of alpha1-antitrypsin: the crystal structure of a cleaved alpha1- antitrypsin polymer.
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