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

The Korean Biophysical Society (한국생물물리학회)
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Probing the movement of helix F region and the stepwise insertion of reactive site loop in $\alpha_1$-Antitrypsin variants

  • Baek, Je-Hyun (21C Frontier R&D Initiative, Functional Proteomics Center, Korea Institute of Science and Technology, Laboratory of Biochemistry, School of Life Sciences ＆ Biotechnology, Korea University) ;
  • Lee, Cheolju (Life Sciences Division, Korea Institute of Science and Technology) ;
  • Kang, Un-Beom (21C Frontier R&D Initiative, Functional Proteomics Center, Korea Institute of Science and Technology, Laboratory of Biochemistry, School of Life Sciences ＆ Biotechnology, Korea University) ;
  • Kim, Joon (Laboratory of Biochemistry, School of Life Sciences & Biotechnology, Korea University) ;
  • Yu, Myeong-Hee (21C Frontier R&D Initiative, Functional Proteomics Center, Korea Institute of Science and Technology)
  • Published : 2003.06.01
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Abstract

$\alpha$$_1$-Antityrpsin is a member of the serine protease inhibitor (SERPIN) family that shares 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. Various biochemical and structural studies suggest that the rate of the RSL insertion upon binding a target protease is critical for inhibitory activity, and it is thought that helix F region (thFs3A and helix F) located in front of $\beta$-sheet A, should be lifted for the loop insertion during complex formation.

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