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

Ben-Gurion University of the Negev

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

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	American 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

All Science Journal Classification (ASJC) codes

Inorganic Chemistry

Access to Document

10.1039/d1qi00284h

Cite this

@article{373798e0e2d142a38579449efbe8a15f,

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.",

author = "Karina Abramov-Harpaz and Yifat Miller",

note = "Publisher Copyright: {\textcopyright} the Partner Organisations.",

year = "2021",

month = jul,

day = "7",

doi = "10.1039/d1qi00284h",

language = "American English",

volume = "8",

pages = "3205--3209",

journal = "Inorganic Chemistry Frontiers",

issn = "2052-1545",

publisher = "Royal Society of Chemistry",

number = "13",

}

TY - JOUR

T1 - A zinc-dependent switching mechanism from an open to a new closed-state conformation of insulin-degrading enzyme

AU - Abramov-Harpaz, Karina

AU - Miller, Yifat

PY - 2021/7/7

Y1 - 2021/7/7

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=85109069059&partnerID=8YFLogxK

U2 - 10.1039/d1qi00284h

DO - 10.1039/d1qi00284h

M3 - Article

SN - 2052-1545

VL - 8

SP - 3205

EP - 3209

JO - Inorganic Chemistry Frontiers

JF - Inorganic Chemistry Frontiers

IS - 13

ER -

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

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this