Distribution and Structural Basis of the Native Strain in Human $\alpha_1$-Antitrypsin

  • Seo, Eun-Joo (National Creative Research Initiative Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Hana Im (National Creative Research Initiative Center, Korea Research Institute of Bioscience and Biotechnolog) ;
  • Maeng, Jin-Soo (National Creative Research Initiative Center, Korea Research Institute of Bioscience and Biotechnolog) ;
  • Kim, Kyoon-Eon (Dept. of Biochemistry, Chungnam National University) ;
  • Yu, Myeong-Hee (National Creative Research Initiative Center, Korea Research Institute of Bioscience and Biotechnology)
  • Published : 1999.06.01

Abstract

Metastability in the native form of proteins has been recognized as a mechanism of biological regulation. The strained native structure of serpins (serine proteinase inhibitors) is a typical example. The native strain of serpins is considered to be crucial to their physiological functions, such as plasma proteinase inhibition, hormone delivery, Alzheimer filament assembly, and extracellular matrix remodeling.(omitted)

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