Allosteric modulation of the binding affinity between PQBP1 and the spliceosomal protein U5-15kD

作者：Mizuguchi Mineyuki^*; Obita Takayuki; Kajiyama Asagi; Kozakai Yuki; Nakai Tsuyoshi; Nabeshima Yuko; Okazawa Hitoshi

来源：FEBS LETTERS, 2016, 590(14): 2221-2231.

DOI：10.1002/1873-3468.12256

• allosteric mechanism
• interaction
• intrinsically disordered protein

Polyglutamine tract-binding protein 1 (PQBP1) is an intrinsically disordered protein composed of a small folded WW domain and a long disordered region. PQBP1 binds to spliceosomal proteins WBP11 and U5-15kD through its N-terminal WW domain and C-terminal region, respectively. Here, we reveal that the binding between PQBP1 and WBP11 reduces the binding affinity between PQBP1 and U5-15kD. Our results suggest that the interaction between PQBP1 and WBP11 negatively modulates the U5-15kD binding of PQBP1 by an allosteric mechanism.

• 出版日期2016-7