Structure of the 14-3-3ζ-LKB1 fusion protein provides insight into a novel ligand-binding mode of 14-3-3

被引：6
|
作者：
Ding, Sheng [1 ]
Zhou, Ruiqing [2 ]
Zhu, Yaqin [1 ]
机构：
[1] Shanghai Jiao Tong Univ, Dept Gen Dent, Shanghai Peoples Hosp 9, Sch Med,Shanghai Key Lab Stomatol, Shanghai 200011, Peoples R China
[2] Shanghai Jiao Tong Univ, Dept Dent, Shanghai Xin Hua Hosp, Sch Med, Shanghai 200092, Peoples R China
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2015年 / 71卷
关键词：
LKB1; tumour supressors; 14-3-3; zeta; crystal structure; KINASE; LKB1;
D O I：
10.1107/S2053230X15012595
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
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 14-3-3 zeta-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.
引用
收藏
页码：1114 / 1119
页数：6
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