The STIL protein contains intrinsically disordered regions that mediate its protein-protein interactions

被引：7
|
作者：
Amartely, Hadar [1 ]
David, Ahuvit [2 ,3 ,4 ]
Lebendiker, Mario [5 ]
Benyamini, Hadar [1 ]
Izraeli, Shai [2 ,3 ,4 ]
Friedler, Assaf [1 ]
机构：
[1] Hebrew Univ Jerusalem, Inst Chem, IL-91904 Jerusalem, Israel
[2] Sheba Canc Res Ctr, IL-52621 Tel Hashomer, Israel
[3] Edmond & Lily Safra Children Hosp, IL-52621 Tel Hashomer, Israel
[4] Tel Aviv Univ, Fac Med, Dept Mol Genet & Biochem, IL-69978 Tel Aviv, Israel
[5] Hebrew Univ Jerusalem, Wolfson Ctr Appl Struct Biol, IL-91904 Jerusalem, Israel
来源：
CHEMICAL COMMUNICATIONS | 2014年 / 50卷 / 40期
基金：
以色列科学基金会; 欧洲研究理事会;
关键词：
BINDING DOMAIN; SIL GENE; HUMAN-CELLS; CANCER; PHOSPHORYLATION; CHECKPOINT; EXPRESSION; LOCUS;
D O I：
10.1039/c3cc45096a
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
The STIL protein participates in mitosis and malignant transformation by regulating centrosomal duplication. Using biophysical methods we studied the structure and interactions of STIL. We revealed that its central domain is intrinsically disordered and mediates protein-protein interactions of STIL. The intrinsic disorder may provide STIL with the conformational flexibility required for its multitude binding.
引用
收藏
页码：5245 / 5247
页数：3
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