The crystal structure of the interleukin 21 receptor bound to interleukin 21 reveals that a sugar chain interacting with the WSXWS motif is an integral part of the interleukin 21 receptor

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The crystal structure of the interleukin 21 receptor bound to interleukin 21 reveals that a sugar chain interacting with the WSXWS motif is an integral part of the interleukin 21 receptor. / Hamming, Ole Jensen; Kang, Lishan; Svensson, Anders; Karlsen, Jesper Lykkegaard; Rahbek-Nielsen, Henrik; Paludan, Søren Riis; Hjorth, Siv A; Bondensgaard, Kent; Hartmann, Rune.

I: Journal of Biological Chemistry, Bind 287, 16.03.2012, s. 9454-9460.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

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Hamming, Ole Jensen ; Kang, Lishan ; Svensson, Anders ; Karlsen, Jesper Lykkegaard ; Rahbek-Nielsen, Henrik ; Paludan, Søren Riis ; Hjorth, Siv A ; Bondensgaard, Kent ; Hartmann, Rune. / The crystal structure of the interleukin 21 receptor bound to interleukin 21 reveals that a sugar chain interacting with the WSXWS motif is an integral part of the interleukin 21 receptor. I: Journal of Biological Chemistry. 2012 ; Bind 287. s. 9454-9460.

Bibtex

@article{043bfcaa6f5d4a07b0af87c240170435,
title = "The crystal structure of the interleukin 21 receptor bound to interleukin 21 reveals that a sugar chain interacting with the WSXWS motif is an integral part of the interleukin 21 receptor",
abstract = "Interleukin (IL) 21 is a class I cytokine, which exerts pleiotropic effects on both innate and adaptive immune responses. It signals through a heterodimeric receptor complex consisting of the IL-21 receptor (IL-21R) and the common gamma chain (gC). A hallmark of the class I cytokine receptors is the class I cytokine receptor signature motif (WSXWS). The exact role of this motif has not been determined yet, however, it has been implicated in diverse functions including ligand binding, receptor internalization, proper folding, and export as well as signal transduction. Furthermore, the WXXW is known to be a consensus sequence for C-mannosylation. Here we present the crystal structure of IL-21 bound to IL-21R and reveal that the WSXWS motif of IL-21R is C-mannosylated on the first tryptophan. We furthermore demonstrate that a sugar chain bridge the two fibronectin domains which constitute the extracellular domain of IL-21R and anchors at the WSXWS motif through an extensive hydrogen bonding network, including the mannosylation. The glycan thus transforms the V-shaped receptor into a A-frame. This finding offers a novel structural explanation of the role of the class I cytokine signature motif",
keywords = "Carbohydrate glycoprotein, Carbohydrate structure, Crystallography, Immunology, Interleukin, Protein structure, Receptor structure-function",
author = "Hamming, {Ole Jensen} and Lishan Kang and Anders Svensson and Karlsen, {Jesper Lykkegaard} and Henrik Rahbek-Nielsen and Paludan, {S{\o}ren Riis} and Hjorth, {Siv A} and Kent Bondensgaard and Rune Hartmann",
year = "2012",
month = mar,
day = "16",
doi = "10.1074/jbc.M111.311084",
language = "English",
volume = "287",
pages = "9454--9460",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",

}

RIS

TY - JOUR

T1 - The crystal structure of the interleukin 21 receptor bound to interleukin 21 reveals that a sugar chain interacting with the WSXWS motif is an integral part of the interleukin 21 receptor

AU - Hamming, Ole Jensen

AU - Kang, Lishan

AU - Svensson, Anders

AU - Karlsen, Jesper Lykkegaard

AU - Rahbek-Nielsen, Henrik

AU - Paludan, Søren Riis

AU - Hjorth, Siv A

AU - Bondensgaard, Kent

AU - Hartmann, Rune

PY - 2012/3/16

Y1 - 2012/3/16

N2 - Interleukin (IL) 21 is a class I cytokine, which exerts pleiotropic effects on both innate and adaptive immune responses. It signals through a heterodimeric receptor complex consisting of the IL-21 receptor (IL-21R) and the common gamma chain (gC). A hallmark of the class I cytokine receptors is the class I cytokine receptor signature motif (WSXWS). The exact role of this motif has not been determined yet, however, it has been implicated in diverse functions including ligand binding, receptor internalization, proper folding, and export as well as signal transduction. Furthermore, the WXXW is known to be a consensus sequence for C-mannosylation. Here we present the crystal structure of IL-21 bound to IL-21R and reveal that the WSXWS motif of IL-21R is C-mannosylated on the first tryptophan. We furthermore demonstrate that a sugar chain bridge the two fibronectin domains which constitute the extracellular domain of IL-21R and anchors at the WSXWS motif through an extensive hydrogen bonding network, including the mannosylation. The glycan thus transforms the V-shaped receptor into a A-frame. This finding offers a novel structural explanation of the role of the class I cytokine signature motif

AB - Interleukin (IL) 21 is a class I cytokine, which exerts pleiotropic effects on both innate and adaptive immune responses. It signals through a heterodimeric receptor complex consisting of the IL-21 receptor (IL-21R) and the common gamma chain (gC). A hallmark of the class I cytokine receptors is the class I cytokine receptor signature motif (WSXWS). The exact role of this motif has not been determined yet, however, it has been implicated in diverse functions including ligand binding, receptor internalization, proper folding, and export as well as signal transduction. Furthermore, the WXXW is known to be a consensus sequence for C-mannosylation. Here we present the crystal structure of IL-21 bound to IL-21R and reveal that the WSXWS motif of IL-21R is C-mannosylated on the first tryptophan. We furthermore demonstrate that a sugar chain bridge the two fibronectin domains which constitute the extracellular domain of IL-21R and anchors at the WSXWS motif through an extensive hydrogen bonding network, including the mannosylation. The glycan thus transforms the V-shaped receptor into a A-frame. This finding offers a novel structural explanation of the role of the class I cytokine signature motif

KW - Carbohydrate glycoprotein

KW - Carbohydrate structure

KW - Crystallography

KW - Immunology

KW - Interleukin

KW - Protein structure

KW - Receptor structure-function

U2 - 10.1074/jbc.M111.311084

DO - 10.1074/jbc.M111.311084

M3 - Journal article

C2 - 22235133

VL - 287

SP - 9454

EP - 9460

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

ER -