Structure of the 14-3-3ζ-LKB1 fusion protein provides insight into a novel ligand-binding mode of 14-3-3.
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.
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.
Sheng
S
Ding
Department of Dentistry, Shanghai Xin Hua Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200092, People's Republic of China.
Ruiqing
R
Zhou
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.
Yaqin
Y
Zhu
D048948:14-3-3 Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D008024:Ligands; D008958:Models, Molecular; D011487:Protein Conformation; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry*; D011993:Recombinant Fusion Proteins / Q000737:chemistry*
D048948:14-3-3 Proteins; D008024:Ligands; D011993:Recombinant Fusion Proteins; D017346:Protein Serine-Threonine Kinases
14-3-3ζ; LKB1; crystal structure; tumour supressors