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Title 

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

Authors 

Myeong Hee YuKee Nyung LeeJeong Ho Kim

Publisher 

Nature Publishing Group

Issue Date 

1995

Citation 

Nature Structural Biology, vol. 2, no. 5, pp. 363-367

Keywords 

alpha 1 antitrypsinalpha 1 antitrypsin deficiencyconformational transitionemphysemahumanpathogenesispriority journalprotein conformationprotein foldingprotein polymerization

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

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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