A zinc-dependent switching mechanism from an open to a new closed-state conformation of insulin-degrading enzyme

Abstract

The switching mechanism between an open-state conformation and a newly closed-state conformation of IDE is stabilized by electrostatic interactions between domain D1 and domain D3. The loss of a Zn²⁺ ion at the catalytic zinc-binding site in the open-state conformation of IDE prevents the transition to the closed-state conformation.