Crystal structure of an uncleaved α 1‐antitrypsin reveals the conformation of its inhibitory reactive loop

FEBS Letters

关键词: α 1-Antitrypsin;    Inhibitory loop;    Molecular replacement;    Serpin;    X-ray structure;    serpins;    serine proteinase inhibitorsc;    α 1AT;    α 1-antitrypsin;    r.m.s.;    root mean square;    9api∗;    modified α 1-antitrypsin with the reactive loop (P15-P5′;    residues 344–363) removed;   

DOI  :  10.1016/0014-5793(95)01331-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The crystal structure of a recombinant human α 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 Å data with good stereochemistry. This structure provides the first view at the inhibitory loop and the central β-sheet A of the uncleaved α ₁-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].

【 授权许可】

Unknown