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

Karina Abramov-Harpaz; Yifat Miller

doi:10.1039/d1qi00284h

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

Karina Abramov-Harpaz, Yifat Miller

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

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.

Original language	English
Pages (from-to)	3205-3209
Number of pages	5
Journal	Inorganic Chemistry Frontiers
Volume	8
Issue number	13
DOIs	https://doi.org/10.1039/d1qi00284h
State	Published - 7 Jul 2021

ASJC Scopus subject areas

Inorganic Chemistry

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title = "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.",

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AB - 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.

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

Abstract

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