High-speed AFM reveals accelerated binding of agitoxin-2 to a K⁺ channel by induced fit.

ABSTRACT: Agitoxin-2 (AgTx2) from scorpion venom is a potent blocker of K⁺ channels. The docking model has been elucidated, but it remains unclear whether binding dynamics are described by a two-state model (AgTx2-bound and AgTx2-unbound) or a more complicated mechanism, such as induced fit or conformational selection. Here, we observed the binding dynamics of AgTx2 to the KcsA channel using high-speed atomic force microscopy. From images of repeated binding and dissociation of AgTx2 to the channel, single-molecule kinetic analyses revealed that the affinity of the channel for AgTx2 increased during persistent binding and decreased during persistent dissociation. We propose a four-state model, including high- and low-affinity states of the channel, with relevant rate constants. An induced

SUBMITTER: Sumino A 

PROVIDER: S-EPMC6609221 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature