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    FEBS Lett. 1995 Dec 18;377(2):150-4.

    Crystal structure of an uncleaved alpha 1-antitrypsin reveals the conformation of its inhibitory reactive loop.

    Song HK, Lee KN, Kwon KS, Yu MH, Suh SW.

    Department of Chemistry, Seoul National University, South Korea.

    The crystal structure of a recombinant human alpha 1-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 A data with good stereochemistry. This structure provides the first view at the inhibitory loop and the central beta-sheet A of the uncleaved alpha 1-antitrypsin. The reactive loop takes a distorted helical conformation and no pre-insertion of two residues in the reactive loop into the beta-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].

    PMID: 8543039 [PubMed - indexed for MEDLINE]

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    Structures reported by this article

    • Alpha1-Antitrypsin
      PDB: 1KCT
      Source: Homo sapiens
      Method: X-Ray Diffraction | Resolution: 3.46 Å

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