14-3-3ζ-LKB1融合蛋白的结构为深入了解14-3-3的新型配体结合模式提供了线索。
Structure of the 14-3-3ζ-LKB1 fusion protein provides insight into a novel ligand-binding mode of 14-3-3.
作者信息
Ding Sheng, Zhou Ruiqing, Zhu Yaqin
机构信息
Department of General Dentistry, Shanghai Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai Key Laboratory of Stomatology, Shanghai 200011, People's Republic of China.
Department of Dentistry, Shanghai Xin Hua Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200092, People's Republic of China.
出版信息
Acta Crystallogr F Struct Biol Commun. 2015 Sep;71(Pt 9):1114-9. doi: 10.1107/S2053230X15012595. Epub 2015 Aug 25.
Abstract
The 14-3-3 proteins are a family of highly conserved proteins that play key roles in many cellular processes. The tumour suppressor LKB1 regulates cell polarity, cell growth and energy metabolism. 14-3-3 proteins bind to LKB1 and suppress its functions. Previously, preliminary crystallographic data for the 14-3-3ζ-LKB1 fusion protein have been reported. Here, the crystal structure of this fusion protein was solved and a novel potential binding mode of 14-3-3 to its ligands was found.
摘要
14-3-3蛋白是一类高度保守的蛋白，在许多细胞过程中发挥关键作用。肿瘤抑制因子LKB1调节细胞极性、细胞生长和能量代谢。14-3-3蛋白与LKB1结合并抑制其功能。此前，已经报道了14-3-3ζ-LKB1融合蛋白的初步晶体学数据。在此，解析了该融合蛋白的晶体结构，并发现了14-3-3与其配体的一种新的潜在结合模式。
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