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...
Main Authors: | , , , , , , , |
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Format: | Article |
Language: | English |
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Public Library of Science (PLoS)
2017-01-01
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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. |
first_indexed | 2024-04-14T07:23:38Z |
format | Article |
id | doaj.art-8e2edc5e8cb347b5a639618e33fae3e7 |
institution | Directory Open Access Journal |
issn | 1932-6203 |
language | English |
last_indexed | 2024-04-14T07:23:38Z |
publishDate | 2017-01-01 |
publisher | Public Library of Science (PLoS) |
record_format | Article |
series | PLoS ONE |
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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