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

Autor(en): Chuartzman, Silvia G.
Nevo, Reinat
Waichman, Sharon
Shental, Dalit
Piehler, Jacob 
Levy, Yaakov
Reich, Ziv
Kapon, Ruti
Stichwörter: ACTIVATION; CYTOKINE; I INTERFERONS; IFN-ALPHA-2; IFNAR1; Multidisciplinary Sciences; MUTATIONAL ANALYSIS; PHAGE DISPLAY; PROTEIN; Science & Technology - Other Topics; SPECTROSCOPY; STRUCTURAL BASIS
Erscheinungsdatum: 2017
Herausgeber: PUBLIC LIBRARY SCIENCE
Journal: PLOS ONE
Volumen: 12
Ausgabe: 4
Zusammenfassung: 
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.
ISSN: 19326203
DOI: 10.1371/journal.pone.0175413

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