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Structure of the 14‐3‐3ζ–LKB1 fusion protein provides insight into a novel ligand‐binding mode of 14‐3‐3
Author(s) -
Ding Sheng,
Zhou Ruiqing,
Zhu Yaqin
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15012595
Subject(s) - fusion protein , fusion , microbiology and biotechnology , ligand (biochemistry) , protein structure , plasma protein binding , protein family , chemistry , suppressor , biology , computational biology , crystallography , biochemistry , receptor , gene , recombinant dna , linguistics , philosophy
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.