3P6H

Human adipocyte lipid-binding protein FABP4 in complex with (S)-ibuprofen

3P6H の概要

• エントリーDOI: 10.2210/pdb3p6h/pdb
• 関連するPDBエントリー: 3P6C 3P6D 3P6E 3P6F 3P6G
• 分子名称: Fatty acid-binding protein, adipocyte, IBUPROFEN (3 entities in total)
• 機能のキーワード: lipocalin, beta barrel, fatty acid binding protein, drug, nonsteroidal anti-inflammatory drug, lipid binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P15090
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15692.01

構造登録者

Gonzalez, J.M.,Pozharski, E. (登録日: 2010-10-11, 公開日: 2011-04-13, 最終更新日: 2024-02-21)

主引用文献

Gonzalez, J.M.,Fisher, S.Z.
Structural analysis of ibuprofen binding to human adipocyte fatty-acid binding protein (FABP4).
Acta Crystallogr F Struct Biol Commun, 71:163-170, 2015

PubMed Abstract: Inhibition of human adipocyte fatty-acid binding protein (FABP4) has been proposed as a treatment for type 2 diabetes, fatty liver disease and atherosclerosis. However, FABP4 displays a naturally low selectivity towards hydrophobic ligands, leading to the possibility of side effects arising from cross-inhibition of other FABP isoforms. In a search for structural determinants of ligand-binding selectivity, the binding of FABP4 towards a group of small molecules structurally related to the nonsteroidal anti-inflammatory drug ibuprofen was analyzed through X-ray crystallography. Several specific hydrophobic interactions are shown to enhance the binding affinities of these compounds, whereas an aromatic edge-to-face interaction is proposed to determine the conformation of bound ligands, highlighting the importance of aromatic interactions in hydrophobic environments.

PubMed: 25664790
DOI: 10.1107/S2053230X14027897

実験手法

X-RAY DIFFRACTION (1.15 Å)