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 |
|---|---|
| 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
Cite this
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Cleaved antitrypsin polymers at atomic resolution. / Dunstone, Michelle A.; Dai, Weiwen; Whisstock, James C.; Rossjohn, Jamie; Pike, Robert N.; Feil, Susanne C.; Le Bonniec, Bernard F.; Parker, Michael W.; Bottomley, Stephen P.
In: Protein Science, Vol. 9, No. 2, 13.03.2000, p. 417-420.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - Cleaved antitrypsin polymers at atomic resolution
AU - Dunstone, Michelle A.
AU - Dai, Weiwen
AU - Whisstock, James C.
AU - Rossjohn, Jamie
AU - Pike, Robert N.
AU - Feil, Susanne C.
AU - Le Bonniec, Bernard F.
AU - Parker, Michael W.
AU - Bottomley, Stephen P.
PY - 2000/3/13
Y1 - 2000/3/13
N2 - 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.
AB - 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.
KW - α-antitrypsin deficiency
KW - Conformational disease
KW - Polymerization
KW - X-ray crystallography
UR - http://www.scopus.com/inward/record.url?scp=0034000728&partnerID=8YFLogxK
M3 - Article
VL - 9
SP - 417
EP - 420
JO - Protein Science
JF - Protein Science
SN - 0961-8368
IS - 2
ER -