Proceedings of the Korean Biophysical Society Conference (한국생물물리학회:학술대회논문집)

The Korean Biophysical Society (한국생물물리학회)
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CRYSTAL STRUCTURE OF AN UNCLEAVED $\alpha_1$-ANTITRYPSIN WITH SEVEN STABILIZING MUTATIONS AT 2.7 $\{AA}$ RESOLUTION

  • Ryu, Seong-Eon (Protein Engineering Research Division Korea Research Institute of Bioscience and Biotechnology, KIST) ;
  • Park, Hee-Jeong (Protein Engineering Research Division Korea Research Institute of Bioscience and Biotechnology, KIS) ;
  • Kwon, Ki-Sun (Protein Engineering Research Division Korea Research Institute of Bioscience and Biotechnology, KIS) ;
  • Lee, Kee-Nyung (Protein Engineering Research Division Korea Research Institute of Bioscience and Biotechnology, KIS) ;
  • Yu, Myung-Hee (Protein Engineering Research Division Korea Research Institute of Bioscience and Biotechnology, KIST)
  • Published : 1996.07.01
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Abstract

$\alpha$$_1$-arantitrypsin, a member of the serpin (serine protease inhibitor) family, undergoes a large structural rearrangement upon the cleavage and insertion of the reactive site loop. This conformational change is driven by the metastability of the native serpin structures and has an important role in the regulation of the inhibitory-serpin function. (omitted)

Keywords