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Structural basis of receptor sharing by interleukin 17 cytokines
T helper type 17 (T(H)-17) cells, together with their effector cytokines including interleukin 17 (IL-17) family members, are emerging as key mediators of chronic inflammatory and autoimmune disorders. Here we present the crystal structure of a 1:2 complex of IL-17RA bound to IL-17F. The manner of c...
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Formato: | Texto |
Lenguaje: | English |
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2009
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2783927/ https://www.ncbi.nlm.nih.gov/pubmed/19838198 http://dx.doi.org/10.1038/ni.1813 |
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author | Ely, Lauren K. Fischer, Suzanne Garcia, K. Christopher |
author_facet | Ely, Lauren K. Fischer, Suzanne Garcia, K. Christopher |
author_sort | Ely, Lauren K. |
collection | PubMed |
description | T helper type 17 (T(H)-17) cells, together with their effector cytokines including interleukin 17 (IL-17) family members, are emerging as key mediators of chronic inflammatory and autoimmune disorders. Here we present the crystal structure of a 1:2 complex of IL-17RA bound to IL-17F. The manner of complex formation is unique for cytokines, and involves two fibronectin-type domains of IL-17RA engaging IL-17 within a groove between the IL-17 homodimer interface in a knob-and-hole fashion. The first receptor-binding event to the IL-17 cytokines modulates the affinity and specificity of the second receptor-binding event, thereby promoting heterodimeric versus homodimeric complex formation. IL-17RA utilizes a common recognition strategy to bind to several IL-17 family members, allowing it to potentially act as a shared receptor within multiple different signaling complexes. |
format | Text |
id | pubmed-2783927 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
record_format | MEDLINE/PubMed |
spelling | pubmed-27839272010-06-01 Structural basis of receptor sharing by interleukin 17 cytokines Ely, Lauren K. Fischer, Suzanne Garcia, K. Christopher Nat Immunol Article T helper type 17 (T(H)-17) cells, together with their effector cytokines including interleukin 17 (IL-17) family members, are emerging as key mediators of chronic inflammatory and autoimmune disorders. Here we present the crystal structure of a 1:2 complex of IL-17RA bound to IL-17F. The manner of complex formation is unique for cytokines, and involves two fibronectin-type domains of IL-17RA engaging IL-17 within a groove between the IL-17 homodimer interface in a knob-and-hole fashion. The first receptor-binding event to the IL-17 cytokines modulates the affinity and specificity of the second receptor-binding event, thereby promoting heterodimeric versus homodimeric complex formation. IL-17RA utilizes a common recognition strategy to bind to several IL-17 family members, allowing it to potentially act as a shared receptor within multiple different signaling complexes. 2009-10-18 2009-12 /pmc/articles/PMC2783927/ /pubmed/19838198 http://dx.doi.org/10.1038/ni.1813 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Ely, Lauren K. Fischer, Suzanne Garcia, K. Christopher Structural basis of receptor sharing by interleukin 17 cytokines |
title | Structural basis of receptor sharing by interleukin 17 cytokines |
title_full | Structural basis of receptor sharing by interleukin 17 cytokines |
title_fullStr | Structural basis of receptor sharing by interleukin 17 cytokines |
title_full_unstemmed | Structural basis of receptor sharing by interleukin 17 cytokines |
title_short | Structural basis of receptor sharing by interleukin 17 cytokines |
title_sort | structural basis of receptor sharing by interleukin 17 cytokines |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2783927/ https://www.ncbi.nlm.nih.gov/pubmed/19838198 http://dx.doi.org/10.1038/ni.1813 |
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