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Protein–protein interaction networks are the networks of protein complexes formed by biochemical events and/or electrostatic forces and that serve a distinct biological function as a complex. The protein interactome describes the full repertoire of a biological system’s protein–protein interactions (PPIs).
Owens et al. reported PFI-7, a selective and potent antagonist of GID4 of the CTLH E3 ligase complex, which enables identification of human GID4 targets. This study provides valuable insights into GID4 functions and a powerful tool for advancing new targeted protein degradation strategies.
The specific recognition of a proline-rich motif in the intrinsically disordered region of SF1 by the PRPF40A tandem WW domains is modulated by an intramolecular autoinhibition, suggesting a general mechanism to enhance WW binding selectivity.
The combination of mass spectroscopy-based proteomics with molecular dynamics enables the in-depth study of metallothioneine-Zn(II) binding mechanisms, critical to cell homeostasis and Zn(II) ion buffering.
Co-fractionation mass spectrometry (CF-MS) has the potential to measure thousands of protein complexes in a single experiment, but the field is still in its infancy. A meta-analysis of CF-MS data yields a core CF-MS interactome and a tool allowing researchers to align new results to published data.