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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.