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. 2018 Apr 17;9:341. doi: 10.3389/fphar.2018.00341

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Copyright © 2018 Janciauskiene, Wrenger, Immenschuh, Olejnicka, Greulich, Welte and Chorostowska-Wynimko.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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3D structure of AAT. The AAT protein is a 394-amino acid peptide with one free cysteine residue (marked in the structure) and three asparagine-linked carbohydrate side-chains at positions 46, 83, and 247. The AAT polypeptide chain is arranged into structural elements consisting of three beta-sheets (blue color) and nine alpha-helices (purple color), each formed by the first 150 residues. A reactive center loop presents the key Met358–Ser359 (P1-P1′) residues for the cleavage by the target proteases. This active site designated “P1 residue” is responsible for the anti-protease activity and specificity of the inhibitor. Side chains of amino acids of interest are colored as carbon (green), oxygen (red), nitrogen (blue), and sulfur (yellow).