3KQ0

Crystal structure of human alpha1-acid glycoprotein

「3BX6」から置き換えられました

3KQ0 の概要

• エントリーDOI: 10.2210/pdb3kq0/pdb
• 関連するPDBエントリー: 3BX6
• 分子名称: Alpha-1-acid glycoprotein 1, (2R)-2,3-dihydroxypropyl acetate, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: plasma protein, glycoprotein, polymorphism, acute phase protein, secreted, pyrrolidone carboxylic acid, lipocalin, signaling protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22850.86

構造登録者

Schiefner, A.,Schonfeld, D.L.,Ravelli, R.B.G.,Mueller, U.,Skerra, A. (登録日: 2009-11-17, 公開日: 2010-02-02, 最終更新日: 2019-12-25)

主引用文献

Schonfeld, D.L.,Ravelli, R.B.,Mueller, U.,Skerra, A.
The 1.8-A crystal structure of alpha1-acid glycoprotein (Orosomucoid) solved by UV RIP reveals the broad drug-binding activity of this human plasma lipocalin.
J.Mol.Biol., 384:393-405, 2008

PubMed Abstract: Alpha(1)-acid glycoprotein (AGP) is an important drug-binding protein in human plasma and, as an acute-phase protein, it has a strong influence on pharmacokinetics and pharmacodynamics of many pharmaceuticals. We report the crystal structure of the recombinant unglycosylated human AGP at 1.8 A resolution, which was solved using the new method of UV-radiation-damage-induced phasing (UV RIP). AGP reveals a typical lipocalin fold comprising an eight-stranded beta-barrel. Of the four loops that form the entrance to the ligand-binding site, loop 1, which connects beta-strands A and B, is among the longest observed so far and exhibits two full turns of an alpha-helix. Furthermore, it carries one of the five N-linked glycosylation sites, while a second one occurs underneath the tip of loop 2. The branched, partly hydrophobic, and partly acidic cavity, together with the presumably flexible loop 1 and the two sugar side chains at its entrance, explains the diverse ligand spectrum of AGP, which is known to vary with changes in glycosylation pattern.

PubMed: 18823996
DOI: 10.1016/j.jmb.2008.09.020

実験手法

X-RAY DIFFRACTION (1.8 Å)