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.
Original language | English |
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Pages (from-to) | 417-420 |
Number of pages | 4 |
Journal | Protein Science |
Volume | 9 |
Issue number | 2 |
Publication status | Published - 13 Mar 2000 |
Keywords
- α-antitrypsin deficiency
- Conformational disease
- Polymerization
- X-ray crystallography