Academic Journal

14-3-3 protein interacts with and affects the structure of RGS domain of regulator of G protein signaling 3 (RGS3)

التفاصيل البيبلوغرافية
العنوان: 14-3-3 protein interacts with and affects the structure of RGS domain of regulator of G protein signaling 3 (RGS3)
المؤلفون: Řežábková, L., Bouřa, E., Herman, P., Večeř, J., Bouřová, L. (Lenka), Šulc, M. (Miroslav), Svoboda, P. (Petr), Obšilová, V. (Veronika), Obšil, T.
سنة النشر: 2010
المجموعة: The Czech Academy of Sciences: Publication Activity (ASEP) / Akademie věd ČR - Publikační činnost
مصطلحات موضوعية: 14-3-3 protein, time-resolved fluorescence, RGS3
الوصف: We have investigated whether the 14-3-3 protein binding affects the structure of RGS3 using the time-resolved tryptophan fluorescence spectroscopy and X-ray protein crystallography. Our results revealed that the 14-3-3 protein binding induces structural changes in both the N-terminal part and the C-terminal RGS domain of phosphorylated RGS3 molecule. The data obtained from the resolution of the crystal structure of the RGS domain suggest that the 14-3-3 protein-induced conformational change affects the region within the G(alpha)-interacting portion of the RGS domain. This can explain the inhibitory effect of the 14-3-3 protein on GAP activity of RGS3
نوع الوثيقة: article in journal/newspaper
اللغة: English
تدمد: 1047-8477
1095-8657
Relation: urn:pissn: 1047-8477; urn:eissn: 1095-8657; http://hdl.handle.net/11104/0185864
DOI: 10.1016/j.jsb.2010.03.009
الاتاحة: https://doi.org/10.1016/j.jsb.2010.03.009
http://hdl.handle.net/11104/0185864
رقم الانضمام: edsbas.4CC67F93
قاعدة البيانات: BASE
الوصف
تدمد:10478477
10958657
DOI:10.1016/j.jsb.2010.03.009