Oncogene proteins articles from across Nature Portfolio

Biophysical analyses based on the crystal structure of PHD2 in complex with HIF2α peptide show that the strength of the interaction between Pacak-Zhuang syndrome-causing HIF2α mutants and PHD2 correlates with disease severity.

The binding interaction between the Shelterin complex protein TPP1 and the human telomerase enzyme can trigger telomerase maintenance, however, the conformational change of TPP1 functional for binding remains underexplored. Here, the authors characterize the structural properties of a group of amino acids named the TEL-patch within TPP1’s oligosaccharide/oligonucleotide-domain by molecular dynamics simulation, time-series analyses, and graph-based networks, revealing their conformational plasticity and allosteric communication networks.

The crosstalk between innate immunity and autophagy plays a critical role in cancer. Here, the authors report that an immune receptor NLRP6 potentiates the PI3K/AKT pathway by selective degradation of p85α. The NLRP6-p85α interaction offers a potential therapeutic target for tumor treatment.

The oncoprotein MYC and the topoisomerases TOP1 and TOP2 form a complex named the ‘topoisome’, which promotes MYC-driven transcription.

Traditional approaches to covalent drug design postulate that noncovalent binding affinity (K_i) should be in the nanomolar range for the lead compound to be attractive. A study by Hansen et al. suggests that covalent K-Ras inhibitors can have weak noncovalent binding affinity yet have fast chemical reactivity (k_inact), because K-Ras enhances the covalent reactivity of bound inhibitor, similarly to how enzymes activate their substrates.