Allosteric modulation of the binding affinity between PQBP1 and the spliceosomal protein U5‐15kD. Issue 14 (28th June 2016)

• Record Type: Journal Article
• Authors: Mizuguchi, Mineyuki; Obita, Takayuki; Kajiyama, Asagi; Kozakai, Yuki; Nakai, Tsuyoshi; Nabeshima, Yuko; Okazawa, Hitoshi
• Is Part Of: FEBS letters. Volume 590:Issue 14(2016)
• Page Start: 2221
• Page End: 2231
• Publication Date: 2016-06-28
• Subjects: allosteric mechanism -- interaction -- intrinsically disordered protein; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.12256
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : 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. Abstract :