Crystal structure of an uncleaved α1‐antitrypsin reveals the conformation of its inhibitory reactive loop
- 18 December 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 377 (2) , 150-154
- https://doi.org/10.1016/0014-5793(95)01331-8
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]Keywords
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