1PSI

Intact recombined alpha1-antitrypsin mutant PHE 51 to LEU

1PSI の概要

• エントリーDOI: 10.2210/pdb1psi/pdb
• 分子名称: ALPHA=1=-ANTITRYPSIN (1 entity in total)
• 機能のキーワード: serpin, serine protease inhibitor, glycoprotein, polymorphism, emphysema, disease mutation, acute phase
• 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: 44406.54

構造登録者

Abrahams, J.P.,Elliott, P.R.,Lomas, D.A.,Carrell, R.W. (登録日: 1996-06-11, 公開日: 1996-12-07, 最終更新日: 2023-08-09)

主引用文献

Elliott, P.R.,Lomas, D.A.,Carrell, R.W.,Abrahams, J.P.
Inhibitory conformation of the reactive loop of alpha 1-antitrypsin.
Nat.Struct.Biol., 3:676-681, 1996

PubMed Abstract: The reactive site loop of the serpin family of serine proteinase inhibitors is flexible and can adopt a number of diverse conformations. A 2.9 A resolution structure of alpha 1-antitrypsin-the principal proteinase inhibitor in human plasma-shows the loop in a stable canonical conformation matching that found in all other families of serine proteinase inhibitors. This unexpected finding in the absence of loop insertion into the body of the molecule favours a two-stage mechanism of inhibition and provides a model for the heparin activation of antithrombin. The beta-pleated strand conformation of the loop also accounts for the polymerization of the serpins in disease and for their association with other beta-sheet structures, most notably the beta-amyloid of Alzheimer's disease.

PubMed: 8756325
DOI: 10.1038/nsb0896-676

実験手法

X-RAY DIFFRACTION (2.92 Å)