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@article{1411420, author = {Kacirova, M. and Nováček, Jiří and Man, P. and Obsilova, V. and Obsil, T.}, article_location = {Bethesda, USA}, article_number = {7}, doi = {http://dx.doi.org/10.1016/j.bpj.2017.02.036}, keywords = {EXCHANGE-MASS-SPECTROMETRY; X-RAY-SCATTERING; INTRINSICALLY DISORDERED PROTEINS; SMALL-ANGLE SCATTERING; TRANSDUCIN BETA-GAMMA; LIGAND-BINDING; BIOLOGICAL MACROMOLECULES; PHOSPHORYLATION; REGULATOR; COMPLEX}, language = {eng}, issn = {0006-3495}, journal = {Biophysical Journal}, title = {Structural Basis for the 14-3-3 Protein-Dependent Inhibition of Phosducin Function}, url = {https://www.sciencedirect.com/science/article/pii/S0006349517302515?via%3Dihub}, volume = {112}, year = {2017} }
TY - JOUR ID - 1411420 AU - Kacirova, M. - Nováček, Jiří - Man, P. - Obsilova, V. - Obsil, T. PY - 2017 TI - Structural Basis for the 14-3-3 Protein-Dependent Inhibition of Phosducin Function JF - Biophysical Journal VL - 112 IS - 7 SP - 1339-1349 EP - 1339-1349 PB - Biophysical Society SN - 00063495 KW - EXCHANGE-MASS-SPECTROMETRY KW - X-RAY-SCATTERING KW - INTRINSICALLY DISORDERED PROTEINS KW - SMALL-ANGLE SCATTERING KW - TRANSDUCIN BETA-GAMMA KW - LIGAND-BINDING KW - BIOLOGICAL MACROMOLECULES KW - PHOSPHORYLATION KW - REGULATOR KW - COMPLEX UR - https://www.sciencedirect.com/science/article/pii/S0006349517302515?via%3Dihub N2 - Phosducin (Pdc) is a conserved phosphoprotein that, when unphosphorylated, binds with high affinity to the complex of bg-subunits of G protein transducin (G(t beta gamma)). The ability of Pdc to bind to G(t beta gamma) is inhibited through its phosphorylation at S54 andS73 within the N-terminaldomain (Pdc-ND) followed by association with the scaffolding protein 14-3-3. However, the molecular basis for the 14-3-3-dependent inhibition of Pdc binding to G(t beta gamma) is unclear. By using small-angle x-ray scattering, high-resolution NMR spectroscopy, and limited proteolysis coupled with mass spectrometry, we show that phosphorylated Pdc and 14-3-3 forma complex in which the Pdc-ND region 45-80, which forms a part of Pdc's G(t beta gamma) binding surface and contains both phosphorylation sites, is restrained within the central channel of the 14-3-3 dimer, with both 14-3-3 binding motifs simultaneously participating in protein association. The N-terminal part of Pdc-NDis likely located outside the central channel of the 14-3-3 dimer, but Pdc residues 20-30, which are also involved in G(t beta gamma) binding, are positioned close to the surface of the 14-3-3 dimer. The C-terminal domain of Pdc is located outside the central channel and its structure is unaffected by the complex formation. These results indicate that the 14-3-3 protein-mediated inhibition of Pdc binding to Gtbg is based on steric occlusion of Pdc's G(t beta gamma) binding surface. ER -
KACIROVA, M., Jiří NOVÁČEK, P. MAN, V. OBSILOVA and T. OBSIL. Structural Basis for the 14-3-3 Protein-Dependent Inhibition of Phosducin Function. \textit{Biophysical Journal}. Bethesda, USA: Biophysical Society, 2017, vol.~112, No~7, p.~1339-1349. ISSN~0006-3495. Available from: https://dx.doi.org/10.1016/j.bpj.2017.02.036.
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