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

Kyu Song 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 journalArticlepeer-review

59 Citations (Scopus)


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
Issue number2
Publication statusPublished - 1995 Dec 18
Externally publishedYes


  • Inhibitory loop
  • Molecular replacement
  • Serpin
  • X-ray structure
  • α-Antitrypsin

ASJC Scopus subject areas

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


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