2HZQ

Crystal structure of human apolipoprotein D (ApoD) in complex with progesterone

2HZQ の概要

• エントリーDOI: 10.2210/pdb2hzq/pdb
• 関連するPDBエントリー: 2HZR
• 分子名称: Apolipoprotein D, PROGESTERONE (3 entities in total)
• 機能のキーワード: lipocalin, beta barrel, bilin-binding protein, transport protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P05090
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20302.56

構造登録者

Eichinger, A.,Skerra, A. (登録日: 2006-08-09, 公開日: 2007-08-14, 最終更新日: 2024-10-30)

主引用文献

Eichinger, A.,Nasreen, A.,Kim, H.J.,Skerra, A.
Structural insight into the dual ligand specificity and mode of high density lipoprotein association of apolipoprotein d.
J.Biol.Chem., 282:31068-31075, 2007

PubMed Abstract: Human apolipoprotein D (ApoD) occurs in plasma associated with high density lipoprotein. Apart from the involvement in lipid metabolism, its binding activity for progesterone and arachidonic acid plays a role in cancer development and neurological diseases. The crystal structures of free ApoD and its complex with progesterone were determined at 1.8A resolution and reveal a lipocalin fold. The narrow, mainly uncharged pocket within the typical beta-barrel accommodates progesterone with its acetyl side chain oriented toward the bottom. The cavity adopts essentially the same shape in the absence of progesterone and allows complexation of arachidonic acid as another cognate ligand. Three of the four extended loops at the open end of the beta-barrel expose hydrophobic side chains, which is an unusual feature for lipocalins and probably effects association with the high density lipoprotein particle by mediating insertion into the lipid phase. This mechanism is in line with an unpaired Cys residue in the same surface region that can form a disulfide cross-link with apolipoprotein A-II.

PubMed: 17699160
DOI: 10.1074/jbc.M703552200

実験手法

X-RAY DIFFRACTION (1.8 Å)