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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 a T. OBSIL. Structural Basis for the 14-3-3 Protein-Dependent Inhibition of Phosducin Function. \textit{Biophysical Journal}. Bethesda, USA: Biophysical Society, 2017, roč.~112, č.~7, s.~1339-1349. ISSN~0006-3495. Dostupné z: https://dx.doi.org/10.1016/j.bpj.2017.02.036.
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