The Z type variation of human α₁-antitrypsin causes a protein folding defect

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Title
The Z type variation of human α₁-antitrypsin causes a protein folding defect
Author(s)
Myeong Hee Yu; Kee Nyung Lee; Jeong Ho Kim
Bibliographic Citation
Nature Structural & Molecular Biology, vol. 2, no. 5, pp. 363-367
Publication Year
1995
Abstract
Emphysema is often associated with the Z type mutation of α1- antitrypsin, which causes aggregation of the molecule in the liver and consequent plasma deficiency. The aggregation appears to be due to loop- sheet polymerization, although why the mutant protein polymerizes in vivo is unclear. Here we show that, unlike wild type antitrypsin, which folds in minutes, the folding of Z type α1-antitrypsin is extremely slow. Once folded, however, the native Z protein shows substantial stability towards urea and incubation at 37 °C. The folding defect in Z antitrypsin leads to accumulation of an intermediate and it is the intermediate rather than the native protein which has a high tendency to aggregate.
ISSN
1072-8368
Publisher
Springer-Nature Pub Group
DOI
http://dx.doi.org/10.1038/nsb0595-363
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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