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首页> 外文期刊>Acta crystallographica. Section D, Structural biology >Crystal structure of human brain-type fatty acidbinding protein FABP7 complexed with palmitic acid
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Crystal structure of human brain-type fatty acidbinding protein FABP7 complexed with palmitic acid

机译：人类脑型脂肪的晶体结构acidbinding蛋白质FABP7包裹着棕榈酸

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摘要

The brain-type fatty acid-binding protein FABP7, which is expressed in astrocytes and neural progenitors, is a member of the intracellular lipid-binding protein family. This protein is not only involved in various cellular functions such as metabolism, inflammation and energy homeostasis, but also in diseases such as cognitive disorders and tumors. Structures of unsaturated fatty acids, such as oleic acid (OA) and docosahexaenoic acid (DHA), bound to FABP7 have been elucidated; however, structures of saturated fatty acids bound to FABP7 remain unknown. To better understand fatty acid recognition, here the crystal structure of human brain-type fatty acid-binding protein FABP7 complexed with palmitic acid (PA), a saturated fatty acid, is reported at a resolution of 1.6 A. The PA bound to the fatty acid-binding pocket of FABP7 assumed a U-shaped conformation. The carboxylate moiety of PA interacted with Tyr129, Arg127 and, via a water bridge, with Arg107 and Thr54, whereas its aliphatic chain was stabilized by hydrophobic interactions with Met21, Leu24, Thr30, Thr37, Pro39, Phe58 and Asp77. Structural comparison showed that PA, OA and DHA exhibited unique binding conformations in the fatty acid-binding pocket, stabilized by distinct amino-acid interactions. The binding of PA to FABP7 exhibits a unique binding conformation when compared with other human FABPs (FABP3-FABP5 and FABP8) expressed in other tissues. Based on the crystal and fatty acid structures, it was suggested that PA, which prefers a linear form in nature, required a greater conformational change in its aliphatic chain to bind to the fatty acid-binding pocket in a U-shaped conformation, compared with the cis configurations of OA or DHA. This, together with the length of the aliphatic chain, was considered to be one of the factors determining the binding affinity of PA to FABP7. These results provide a better understanding of fatty acid recognition by FABP7 and expand the knowledge of the binding of PA to FABPs.
机译：脑型脂肪酸结合蛋白FABP7,这是表示在星形胶质细胞和神经祖细胞,是细胞内的一员lipid-binding蛋白质家族。只有参与多种细胞功能代谢、炎症和能量体内平衡,还在等疾病认知障碍和肿瘤。等不饱和脂肪酸,油酸(OA)二十二碳六烯酸(DHA),必定FABP7已被阐明;饱和脂肪酸绑定到FABP7依然存在未知的。识别,这里人类的晶体结构脑型脂肪酸结合蛋白FABP7包裹着棕榈酸(PA),饱和脂肪酸,据报道在1.6的决议。巴勒斯坦权力机构绑定到脂肪酸结合口袋的FABP7假定一个u型的构象。羧酸盐PA与Tyr129互动的一部分,Arg127,通过水桥,Arg107和Thr54,而脂肪链稳定通过疏水相互作用Met21 Leu24,Thr30、Thr37 Pro39, Phe58 Asp77。比较表明,PA, OA和DHA展出独特的结合构象的脂肪结合口袋里,由不同的稳定氨基酸的相互作用。一个独特的结合构象当FABP7展品与其他人类FABPs (FABP3-FABP5相比在其他组织FABP8)表示。水晶和脂肪酸结构,爸爸的建议,更喜欢一个线性形式自然,需要更大的构象变化在脂肪链绑定到脂肪在u型构象结合口袋,相比之下,OA的顺式构型或DHA。脂肪链,被认为是其中一个因素决定PA的亲和力FABP7。FABP7脂肪酸识别的理解和扩大的知识考评的绑定

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