4LKP

Crystal Structure of Apo Human Epidermal Fatty Acid Binding Protein (FABP5)

4LKP の概要

• エントリーDOI: 10.2210/pdb4lkp/pdb
• 関連するPDBエントリー: 4LKT
• 分子名称: Fatty acid-binding protein, epidermal, CHLORIDE ION, DIMETHYL SULFOXIDE, ... (6 entities in total)
• 機能のキーワード: beta barrel, beta clam, fatty acid binding protein, fatty acids, nucleus, lipid binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q01469
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15763.53

構造登録者

Armstrong, E.H.,Ortlund, E.A. (登録日: 2013-07-08, 公開日: 2014-03-26, 最終更新日: 2024-10-16)

主引用文献

Armstrong, E.H.,Goswami, D.,Griffin, P.R.,Noy, N.,Ortlund, E.A.
Structural basis for ligand regulation of the fatty acid-binding protein 5, peroxisome proliferator-activated receptor beta / delta (FABP5-PPAR beta / delta ) signaling pathway.
J.Biol.Chem., 289:14941-14954, 2014

PubMed Abstract: Fatty acid-binding proteins (FABPs) are a widely expressed group of calycins that play a well established role in solubilizing cellular fatty acids. Recent studies, however, have recast FABPs as active participants in vital lipid-signaling pathways. FABP5, like its family members, displays a promiscuous ligand binding profile, capable of interacting with numerous long chain fatty acids of varying degrees of saturation. Certain "activating" fatty acids induce the protein's cytoplasmic to nuclear translocation, stimulating PPARβ/δ transactivation; however, the rules that govern this process remain unknown. Using a range of structural and biochemical techniques, we show that both linoleic and arachidonic acid elicit FABP5's translocation by permitting allosteric communication between the ligand-sensing β2 loop and a tertiary nuclear localization signal within the α-helical cap of the protein. Furthermore, we show that more saturated, nonactivating fatty acids inhibit nuclear localization signal formation by destabilizing this activation loop, thus implicating FABP5 specifically in cis-bonded, polyunsaturated fatty acid signaling.

PubMed: 24692551
DOI: 10.1074/jbc.M113.514646

実験手法

X-RAY DIFFRACTION (1.67 Å)