Charybdotoxin, a toxin produced by scorpions, blocks a K+ channel by binding in a lock-and-key fashion to the mouth of the channel and presenting a lysine amino group, which serves as a K+ mimic in the selectivity filter.
The structures of Slo1 in complex with b4 imply that the auxiliary beta subunits modulate the channel's gating properties through stabilizing ‘pre-existing’ conformations rather than creating new ones.
Different developmental stages of a venomous animal (e.g. Nematostella vectensis) with a complex life cycle produce vastly different venoms that can serve in different antagonistic interactions with other species.
Detection of unbinding transitional states in the charybdotoxin first-order dissociation from a Kv-channel reveals that the bound neurotoxin wobbles, suggesting diverse intermediates and dissociation pathways in this protein–protein interaction.
Plants and humans use a shared mechanism, the eukaryotic metabolic sensor TARGET OF RAPAMYCIN protein kinase and its substrate, an RNA-binding protein called LARP1, to coordinate post-transcriptional gene expression.