Binding of interferon reduces the force of unfolding for interferon receptor 1.

Differential signaling of the type I interferon receptor (IFNAR) has been correlated with the ability of its subunit, IFNAR1, to differentially recognize a large spectrum of different ligands, which involves intricate conformational re-arrangements of multiple interacting domains. To shed light onto...

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Main Authors: Silvia G Chuartzman, Reinat Nevo, Sharon Waichman, Dalit Shental, Jacob Piehler, Yaakov Levy, Ziv Reich, Ruti Kapon
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2017-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC5389645?pdf=render
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author Silvia G Chuartzman
Reinat Nevo
Sharon Waichman
Dalit Shental
Jacob Piehler
Yaakov Levy
Ziv Reich
Ruti Kapon
author_facet Silvia G Chuartzman
Reinat Nevo
Sharon Waichman
Dalit Shental
Jacob Piehler
Yaakov Levy
Ziv Reich
Ruti Kapon
author_sort Silvia G Chuartzman
collection DOAJ
description Differential signaling of the type I interferon receptor (IFNAR) has been correlated with the ability of its subunit, IFNAR1, to differentially recognize a large spectrum of different ligands, which involves intricate conformational re-arrangements of multiple interacting domains. To shed light onto the structural determinants governing ligand recognition, we compared the force-induced unfolding of the IFNAR1 ectodomain when bound to interferon and when free, using the atomic force microscope and steered molecular dynamics simulations. Unexpectedly, we find that IFNAR1 is easier to mechanically unfold when bound to interferon than when free. Analysis of the structures indicated that the origin of the reduction in unfolding forces is a conformational change in IFNAR1 induced by ligand binding.
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spelling doaj.art-8e2edc5e8cb347b5a639618e33fae3e72022-12-22T02:06:04ZengPublic Library of Science (PLoS)PLoS ONE1932-62032017-01-01124e017541310.1371/journal.pone.0175413Binding of interferon reduces the force of unfolding for interferon receptor 1.Silvia G ChuartzmanReinat NevoSharon WaichmanDalit ShentalJacob PiehlerYaakov LevyZiv ReichRuti KaponDifferential signaling of the type I interferon receptor (IFNAR) has been correlated with the ability of its subunit, IFNAR1, to differentially recognize a large spectrum of different ligands, which involves intricate conformational re-arrangements of multiple interacting domains. To shed light onto the structural determinants governing ligand recognition, we compared the force-induced unfolding of the IFNAR1 ectodomain when bound to interferon and when free, using the atomic force microscope and steered molecular dynamics simulations. Unexpectedly, we find that IFNAR1 is easier to mechanically unfold when bound to interferon than when free. Analysis of the structures indicated that the origin of the reduction in unfolding forces is a conformational change in IFNAR1 induced by ligand binding.http://europepmc.org/articles/PMC5389645?pdf=render
spellingShingle Silvia G Chuartzman
Reinat Nevo
Sharon Waichman
Dalit Shental
Jacob Piehler
Yaakov Levy
Ziv Reich
Ruti Kapon
Binding of interferon reduces the force of unfolding for interferon receptor 1.
PLoS ONE
title Binding of interferon reduces the force of unfolding for interferon receptor 1.
title_full Binding of interferon reduces the force of unfolding for interferon receptor 1.
title_fullStr Binding of interferon reduces the force of unfolding for interferon receptor 1.
title_full_unstemmed Binding of interferon reduces the force of unfolding for interferon receptor 1.
title_short Binding of interferon reduces the force of unfolding for interferon receptor 1.
title_sort binding of interferon reduces the force of unfolding for interferon receptor 1
url http://europepmc.org/articles/PMC5389645?pdf=render
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