1ATU

UNCLEAVED ALPHA-1-ANTITRYPSIN

1ATU の概要

• エントリーDOI: 10.2210/pdb1atu/pdb
• 分子名称: ALPHA-1-ANTITRYPSIN (1 entity in total)
• 機能のキーワード: serine protease inhibitor, alpha-1-antitrypsin, conformational transition, loop flexibility, metastability, stabilizing mutations
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted. Short peptide from AAT: Secreted, extracellular space, extracellular matrix: P01009
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42046.09

構造登録者

Ryu, S.-E.,Choi, H.-J. (登録日: 1997-05-11, 公開日: 1997-08-20, 最終更新日: 2024-05-22)

主引用文献

Ryu, S.E.,Choi, H.J.,Kwon, K.S.,Lee, K.N.,Yu, M.H.
The native strains in the hydrophobic core and flexible reactive loop of a serine protease inhibitor: crystal structure of an uncleaved alpha1-antitrypsin at 2.7 A.
Structure, 4:1181-1192, 1996

PubMed Abstract: The protein alpha1-antitrypsin is a prototype member of the serpin (serine protease inhibitor) family and is known to inhibit the activity of neutrophil elastase in the lower respiratory tract. Members of this family undergo a large structural rearrangement upon binding to a target protease, involving cleavage of the reactive-site loop. This loop is then inserted into the main body of the enzyme following the opening of a central beta sheet, leading to stabilization of the structure. Random mutageneses of alpha1-antitrypsin identified various mutations that stabilize the native structure and retard the insertion of the reactive-site loop. Structural studies of these mutations may reveal the mechanism of the conformational change.

PubMed: 8939743
DOI: 10.1016/S0969-2126(96)00126-8

実験手法

X-RAY DIFFRACTION (2.7 Å)