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

Mineyuki Mizuguchi*, Takayuki Obita, Asagi Kajiyama, Yuki Kozakai, Tsuyoshi Nakai, Yuko Nabeshima, Hitoshi Okazawa

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

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.

Original languageEnglish
Pages (from-to)2221-2231
Number of pages11
JournalFEBS Letters
DOIs
StatePublished - 2016/07/01

Keywords

  • allosteric mechanism
  • interaction
  • intrinsically disordered protein

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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