Structural and Computational Biology Group, International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Road, 110067 New Delhi, India.
J Biol Chem. 2011 Sep 9;286(36):31924-8. doi: 10.1074/jbc.M111.270165. Epub 2011 Jul 8.
We crystallized human liver fatty acid-binding protein (LFABP) in apo, holo, and intermediate states of palmitic acid engagement. Structural snapshots of fatty acid recognition, entry, and docking within LFABP support a heads-in mechanism for ligand entry. Apo-LFABP undergoes structural remodeling, where the first palmitate ingress creates the atomic environment for placement of the second palmitate. These new mechanistic insights will facilitate development of pharmacological agents against LFABP.
我们将人肝脂肪酸结合蛋白(LFABP)在 apo、holo 和棕榈酸结合的中间状态下进行结晶。脂肪酸识别、进入和与 LFABP 对接的结构快照支持配体进入的头部向内机制。apo-LFABP 经历结构重塑,其中第一个棕榈酸进入创造了第二个棕榈酸放置的原子环境。这些新的机制见解将有助于开发针对 LFABP 的药物。