Title: Allosteric modulation of the binding affinity between PQBP1 and the spliceosomal protein U5-15kD. | Journal: FEBS letters. 2016 Jul;590(14):2221-31 | Authors: Mizuguchi M, Obita T, Kajiyama A, Kozakai Y, Nakai T, Nabeshima Y, Okazawa H. | 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. | See full PubMed entry: http://www.ncbi.nlm.nih.gov/pubmed/27314904 |
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