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.

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.

The tarantula toxins psalmotoxin and guangxitoxin have a similar concave surface for interacting with α-helices in voltage-gated and acid-sensing ion channels.

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.

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.

The spider venom peptide Pn3a recognizes a pharmacophore unique to Ca_V3.3 amongst T-type calcium channels, underscoring its potential as a novel molecular tool for the study of Ca_V3.3-mediated currents in native cells.

X-ray crystallography reveals new conceptual insights into the location of the β2-subunit in the Na_v channel signaling complex.

Potassium ions enter and leave human sperm cells via a calcium-dependent ion channel that is also pH-independent.

The structure of a bivalent double-knot tarantula toxin bound to the outer pore of the capsaicin receptor reveals a novel mode of toxin-channel recognition that has important implications for thermosensation.