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

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Title
Crystal structure of an uncleaved α₁-antitrypsin reveals the conformation of its inhibitory reactive loop
Author(s)
H K Song; Kee Nyung Lee; Ki Sun Kwon; Myeong Hee Yu; S W Suh
Bibliographic Citation
FEBS Letters, vol. 377, no. 2, pp. 150-154
Publication Year
1995
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 A 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].
Keyword
α1-antitrypsininhibitory loopmolecular replacementserpinx-ray structure
ISSN
0014-5793
Publisher
Wiley
DOI
http://dx.doi.org/10.1016/0014-5793(95)01331-8
Type
Article
Appears in Collections:
Aging Convergence Research Center > 1. Journal Articles
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