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Comment
. 2022 Apr 5;121(7):1115-1116.
doi: 10.1016/j.bpj.2022.03.007. Epub 2022 Mar 9.

Challenges of studying 14-3-3 protein-protein interactions with full-length protein partners

Bente A Somsen  1 , Christian Ottmann  2
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Challenges of studying 14-3-3 protein-protein interactions with full-length protein partners

Bente A Somsen et al. Biophys J. .
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Figure 1
Figure 1
Methods to study 14-3-3/partner protein complexes. (a) Schematic representation of multi-domain phosphorylated protein (green) binding to 14-3-3 (gray), raising the question of structure and mechanism of action. (b) First-line techniques to look at mechanism and structure are cryo-EM and x-ray crystallography. Example of crystal structure of 14-3-3 (gray) with BRAF (red) (PDB: 6U2H). (c) Alternatives to study PPIs in the absence of structural data including fluorophore labeling of individual domains as used by Joshi et al. To see this figure in color, go online.
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