Bernardo I. Pinto

This study determines the structure of Kv channels bound to 4AP, showing it binds the closed state and enters via membrane-facing fenestrations, explaining its inhibitory mechanism.

The paper determines the cryo-EM structure of a Shaker K+ channel mutant and shows that voltage sensing domain activation induces a dynamic shift in the linker population equilibrium rather than directly pulling the gate open.

The paper presents a structural model of the closed Shaker potassium channel, revealing how voltage sensor movement drives pore opening and identifies a binding site for dalfampridine.

This study shows that a single mutation can drastically alter the temperature response of Kv channels by modifying their electromechanical coupling.