Issue 13, 2021

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.

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

Supplementary files

Article information

Article type
Research Article
Submitted
04 Mar 2021
Accepted
05 May 2021
First published
06 May 2021

Inorg. Chem. Front., 2021,8, 3205-3209

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

K. Abramov-Harpaz and Y. Miller, Inorg. Chem. Front., 2021, 8, 3205 DOI: 10.1039/D1QI00284H

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