Crystal structure of an uncleaved α1-antitrypsin reveals the conformation of its inhibitory reactive loop

Hyun Kyu Song, Nyung Lee Kee Nyung Lee, Kwon Ki-Sun Kwon, Yu Myeong-Hee Yu, Won Suh Se Won Suh

Research output: Contribution to journalArticle

58 Citations (Scopus)

Abstract

The crystal structure of a recombinant human α1-antitrypsin, in the uncleaved and uncomplexed state, has been determined by X-ray crystallographic methods and refined to an R-factor of 18.4% for 8.0-3.46 Å data with good stereochemistry. This structure provides the first view at the inhibitory loop and the central β-sheet A of the uncleaved α1-antitrypsin. The reactive loop takes a distorted helical conformation and no pre-insertion of two residues in the reactive loop into the β-sheet A is observed. The present structure is largely in agreement with the model predicted by Engh, Wright, and Huber [Prot. Eng. 3 (1990) 469-477].

Original languageEnglish
Pages (from-to)150-154
Number of pages5
JournalFEBS Letters
Volume377
Issue number2
Publication statusPublished - 1995 Dec 18
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology
  • Genetics
  • Cell Biology
  • Biophysics
  • Biochemistry

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    Song, H. K., Kee Nyung Lee, N. L., Ki-Sun Kwon, K., Myeong-Hee Yu, Y., & Se Won Suh, W. S. (1995). Crystal structure of an uncleaved α1-antitrypsin reveals the conformation of its inhibitory reactive loop. FEBS Letters, 377(2), 150-154.