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

التفاصيل البيبلوغرافية
العنوان: Allosteric modulation of the binding affinity between PQBP1 and the spliceosomal protein U5-15kD
المؤلفون: Yuki Kozakai, Yuko Nabeshima, Takayuki Obita, Mineyuki Mizuguchi, Asagi Kajiyama, Hitoshi Okazawa, Tsuyoshi Nakai
المصدر: FEBS letters. 590(14)
سنة النشر: 2016
مصطلحات موضوعية: 0301 basic medicine, Allosteric regulation, Protein domain, Biophysics, Plasma protein binding, 030105 genetics & heredity, Biochemistry, WW domain, 03 medical and health sciences, Allosteric Regulation, Protein Domains, Structural Biology, Genetics, Humans, Nuclear protein, Molecular Biology, Ribonucleoprotein, U5 Small Nuclear, biology, Nuclear Proteins, Cell Biology, DNA-Binding Proteins, Crystallography, 030104 developmental biology, WBP11, Allosteric enzyme, biology.protein, RNA Splicing Factors, Carrier Proteins, Binding domain, Protein Binding
الوصف: 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.
تدمد: 1873-3468
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a6b913118153347e4108f06a1ec689d
https://pubmed.ncbi.nlm.nih.gov/27314904
حقوق: CLOSED
رقم الأكسشن: edsair.doi.dedup.....9a6b913118153347e4108f06a1ec689d
قاعدة البيانات: OpenAIRE
الوصف
تدمد:18733468