首页> 外文期刊>Nature structural biology >THE Z TYPE VARIATION OF HUMAN ALPHA(1)-ANTITRYPSIN CAUSES A PROTEIN FOLDING DEFECT
【24h】

THE Z TYPE VARIATION OF HUMAN ALPHA(1)-ANTITRYPSIN CAUSES A PROTEIN FOLDING DEFECT

机译:人α(1)-抗胰蛋白酶的Z型变异导致蛋白质折叠缺陷

获取原文
获取原文并翻译 | 示例
           

摘要

Emphysema is often associated with the Z type mutation of alpha(1)-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 alpha(1)-antitrypsin is extremely slow. Once folded, however, the native Z protein shows substantial stability towards urea and incubation at 37 degrees 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. [References: 30]
机译:肺气肿通常与α(1)-抗胰蛋白酶的Z型突变相关,这会导致分子在肝脏中聚集并导致血浆缺乏。尽管尚不清楚突变蛋白在体内聚合的原因,但聚集似乎是由于环板聚合所致。在这里我们显示出,与野生型抗胰蛋白酶在几分钟内折叠不同,Z型alpha(1)-抗胰蛋白酶的折叠非常缓慢。然而,一旦折叠,天然Z蛋白对尿素和在37摄氏度的温育下显示出相当大的稳定性。Z抗胰蛋白酶中的折叠缺陷会导致中间体的积累,它是中间体而不是天然蛋白,具有很高的聚集趋势。 [参考:30]

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号