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A conjugate generated by expressed protein ligation between an antibody targeting dendritic cells (DCs) and an immune-stimulating double-stranded DNA reveals that DCs can mediate both innate and adaptive immunity and represents its potential utility as a vaccine adjuvant.
NMR structures of the homodimeric repressor protein CylR2 collected from 25 °C to –16 °C provide glimpses of the molecular changes that occur during cold denaturation, yielding insights into protein folding and oligomerization.
Optovin is a small molecule that renders zebrafish embryos responsive to light through generation of singlet oxygen and activation of the TrpA1b channel, providing a new tool for optogenetics.
Structural analyses reveal that CopA and CupA share a binuclear Cu(I) ion binding motif and that copper is trafficked from a low-affinity site on CupA to a high-affinity site in CopA, making CupA the first membrane-bound copper chaperone important in copper resistance.
A new protein engineering approach inserts metal-coordination motifs to stabilize natural protein interfaces while other favorable contacts are removed, yielding metal-inducible protein-protein interactions that have allowed the study of a self-assembling protein cage and the chemical labeling of its interior.
π-stacking interactions unique between residues of PUMA and Bcl-xL, which lead to the unfolding of Bcl-xL via an allosteric mechanism, are required to disrupt p53–Bcl-xL interaction and induce apoptosis. This is the first example of regulated protein unfolding for signal transmission.
Methylation of lysine residues regulates chromatin function in part by recruiting readers to these marks. UNC1215, a selective antagonist of the methyllysine reader L3MBTL3 with a polyvalent mode of interaction, reveals BCLAF1 as a methyllysine-dependent interaction partner for L3MBTL3.
