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

FEBS Lett.2016 Jul;590(14):2221-31. doi:10.1002/1873-3468.12256. Epub 2016 Jun 28

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摘要

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.

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

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