Allosteric modulation of the binding affinity between  PQBP 1 and the spliceosomal protein U5‐15kD | Zendy

Mizuguchi Mineyuki | Zendy; Obita Takayuki | Zendy; Kajiyama Asagi | Zendy; Kozakai Yuki | Zendy; Nakai Tsuyoshi | Zendy; Nabeshima Yuko | Zendy; Okazawa Hitoshi | Zendy

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Allosteric modulation of the binding affinity between PQBP 1 and the spliceosomal protein U5‐15kD

Author(s) -

Mizuguchi Mineyuki,

Obita Takayuki,

Kajiyama Asagi,

Kozakai Yuki,

Nakai Tsuyoshi,

Nabeshima Yuko,

Okazawa Hitoshi

Publication year - 2016

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1002/1873-3468.12256

Subject(s) - allosteric regulation , c terminus , chemistry , biophysics , biochemistry , biology , amino acid , receptor

Polyglutamine tract‐binding protein 1 ( PQBP 1) is an intrinsically disordered protein composed of a small folded WW domain and a long disordered region. PQBP 1 binds to spliceosomal proteins WBP 11 and U5‐15kD through its N‐terminal WW domain and C‐terminal region, respectively. Here, we reveal that the binding between PQBP 1 and WBP 11 reduces the binding affinity between PQBP 1 and U5‐15kD. Our results suggest that the interaction between PQBP 1 and WBP 11 negatively modulates the U5‐15kD binding of PQBP 1 by an allosteric mechanism.

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