Probing the Movement of Helix F of $\alpha_1$-Antitrypsin

  • Baek, Je-Hyun (National Creative Research Initiatives, Protein Strain Research Center, Korea Institute of Science and Technology) ;
  • Kim, Jun (Biochemistry, Department of Life & Biotechnology, Korea University) ;
  • Yu, Myeong-Hee (National Creative Research Initiatives, Protein Strain Research Center, Korea Institute of Science and Technology)
  • Published : 2002.06.01

Abstract

$\alpha$$_1$-Antitrypsin is a member of the serine protease inhibitor (serpin) family that share a common tertiary structure. The reactive site loop (RSL) of serpins is exposed at one end of the molecule for protease binding. Upon cleavage by a target protease, the RSL is inserted into the major $\beta$-sheet A, which is a necessary process for formation of a tight inhibitory complex.(omitted)

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