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本文引用的文献

1
Processing of X-ray diffraction data collected in oscillation mode.振荡模式下收集的X射线衍射数据的处理。
Methods Enzymol. 1997;276:307-26. doi: 10.1016/S0076-6879(97)76066-X.
2
Crystallization and preliminary crystallographic analysis of the chimeric protein LKB1-14-3-3ζ.嵌合蛋白LKB1-14-3-3ζ的结晶及初步晶体学分析
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1371-3. doi: 10.1107/S1744309113029230. Epub 2013 Nov 29.
3
14-3-3 interacts with LKB1 via recognizing phosphorylated threonine 336 residue and suppresses LKB1 kinase function.14-3-3 通过识别磷酸化的丝氨酸 336 残基与 LKB1 相互作用,并抑制 LKB1 激酶功能。
FEBS Lett. 2012 Apr 24;586(8):1111-9. doi: 10.1016/j.febslet.2012.03.018. Epub 2012 Mar 23.
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Towards automated crystallographic structure refinement with phenix.refine.利用phenix.refine实现自动化晶体学结构精修
Acta Crystallogr D Biol Crystallogr. 2012 Apr;68(Pt 4):352-67. doi: 10.1107/S0907444912001308. Epub 2012 Mar 16.
5
AMPK: a nutrient and energy sensor that maintains energy homeostasis.AMPK:一种营养和能量传感器,可维持能量平衡。
Nat Rev Mol Cell Biol. 2012 Mar 22;13(4):251-62. doi: 10.1038/nrm3311.
6
14-3-3 proteins as signaling integration points for cell cycle control and apoptosis.14-3-3 蛋白作为细胞周期控制和细胞凋亡的信号整合点。
Semin Cell Dev Biol. 2011 Sep;22(7):688-95. doi: 10.1016/j.semcdb.2011.09.008. Epub 2011 Sep 14.
7
Structural basis of 14-3-3 protein functions.14-3-3 蛋白功能的结构基础。
Semin Cell Dev Biol. 2011 Sep;22(7):663-72. doi: 10.1016/j.semcdb.2011.09.001. Epub 2011 Sep 6.
8
The 14-3-3 proteins in regulation of cellular metabolism.14-3-3 蛋白在细胞代谢调节中的作用。
Semin Cell Dev Biol. 2011 Sep;22(7):713-9. doi: 10.1016/j.semcdb.2011.08.008. Epub 2011 Aug 22.
9
14-3-3 Proteins: diverse functions in cell proliferation and cancer progression.14-3-3 蛋白:在细胞增殖和癌症进展中的多种功能。
Semin Cell Dev Biol. 2011 Sep;22(7):681-7. doi: 10.1016/j.semcdb.2011.08.009. Epub 2011 Aug 22.
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Features and development of Coot.Coot的特点与发展
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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.

DOI:10.1107/S2053230X15012595
PMID:26323294
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4555915/
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。