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Title 

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

Authors 

H K SongKee Nyung LeeKi Sun KwonMyeong Hee YuS W Suh

Publisher 

Elsevier

Issue Date 

1995

Citation 

FEBS Letters, vol. 377, no. 2, pp. 150-154

Keywords 

α1-antitrypsininhibitory loopmolecular replacementserpinx-ray structurealpha 1 antitrypsinprotein conformation

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].

ISSN 

0014-5793

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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