Structural model of human IL-13 defines the spatial interactions with the IL-13Rα/IL-4Rα receptor

J. Zuegg; D. C. Webb; P. S. Foster; M. G. Casarotto

doi:10.1046/j.1440-1711.2001.01035.x

Structural model of human IL-13 defines the spatial interactions with the IL-13Rα/IL-4Rα receptor

J. Zuegg, D. C. Webb, P. S. Foster, M. G. Casarotto^*

^*Corresponding author for this work

John Curtin School of Medical Research

Research output: Contribution to journal › Article › peer-review

7 Citations (Scopus)

Abstract

Interleukin-13 (IL-13) plays a key role in immune responses and inflammation. A structural model of human IL-13 (HuIL-13) based on the nuclear magnetic resonance and X-ray structure of IL-4 is put forward. Unlike previous models, this model is based on new sequence alignments that take into account the formation of the two disulfide linkages that have been determined experimentally. The proposed structure of human IL-13 is similar to IL-4, consisting of a four helix bundle with hydrophobic residues lining the core of the molecule and surface polar residues showing a high degree of solvent accessibility. Regions of HuIL-13 that are critical for the interaction with its receptors are explored and discussed in relation to existing mutagenic studies. From these studies we predict that helices A and C of HuIL-13 interact with the IL-4 receptor alpha (IL-4Rα) region and helix D is responsible for the interaction with the IL-13 receptor alpha 1 (IL-13Rα 1) receptor.

Original language	English
Pages (from-to)	332-339
Number of pages	8
Journal	Immunology and Cell Biology
Volume	79
Issue number	4
DOIs	https://doi.org/10.1046/j.1440-1711.2001.01035.x
Publication status	Published - 2001

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title = "Structural model of human IL-13 defines the spatial interactions with the IL-13Rα/IL-4Rα receptor",

abstract = "Interleukin-13 (IL-13) plays a key role in immune responses and inflammation. A structural model of human IL-13 (HuIL-13) based on the nuclear magnetic resonance and X-ray structure of IL-4 is put forward. Unlike previous models, this model is based on new sequence alignments that take into account the formation of the two disulfide linkages that have been determined experimentally. The proposed structure of human IL-13 is similar to IL-4, consisting of a four helix bundle with hydrophobic residues lining the core of the molecule and surface polar residues showing a high degree of solvent accessibility. Regions of HuIL-13 that are critical for the interaction with its receptors are explored and discussed in relation to existing mutagenic studies. From these studies we predict that helices A and C of HuIL-13 interact with the IL-4 receptor alpha (IL-4Rα) region and helix D is responsible for the interaction with the IL-13 receptor alpha 1 (IL-13Rα 1) receptor.",

keywords = "Asthma, Cytokine, Homology modelling, Interleukin-13",

author = "J. Zuegg and Webb, {D. C.} and Foster, {P. S.} and Casarotto, {M. G.}",

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doi = "10.1046/j.1440-1711.2001.01035.x",

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T1 - Structural model of human IL-13 defines the spatial interactions with the IL-13Rα/IL-4Rα receptor

AU - Zuegg, J.

AU - Webb, D. C.

AU - Foster, P. S.

AU - Casarotto, M. G.

PY - 2001

Y1 - 2001

N2 - Interleukin-13 (IL-13) plays a key role in immune responses and inflammation. A structural model of human IL-13 (HuIL-13) based on the nuclear magnetic resonance and X-ray structure of IL-4 is put forward. Unlike previous models, this model is based on new sequence alignments that take into account the formation of the two disulfide linkages that have been determined experimentally. The proposed structure of human IL-13 is similar to IL-4, consisting of a four helix bundle with hydrophobic residues lining the core of the molecule and surface polar residues showing a high degree of solvent accessibility. Regions of HuIL-13 that are critical for the interaction with its receptors are explored and discussed in relation to existing mutagenic studies. From these studies we predict that helices A and C of HuIL-13 interact with the IL-4 receptor alpha (IL-4Rα) region and helix D is responsible for the interaction with the IL-13 receptor alpha 1 (IL-13Rα 1) receptor.

AB - Interleukin-13 (IL-13) plays a key role in immune responses and inflammation. A structural model of human IL-13 (HuIL-13) based on the nuclear magnetic resonance and X-ray structure of IL-4 is put forward. Unlike previous models, this model is based on new sequence alignments that take into account the formation of the two disulfide linkages that have been determined experimentally. The proposed structure of human IL-13 is similar to IL-4, consisting of a four helix bundle with hydrophobic residues lining the core of the molecule and surface polar residues showing a high degree of solvent accessibility. Regions of HuIL-13 that are critical for the interaction with its receptors are explored and discussed in relation to existing mutagenic studies. From these studies we predict that helices A and C of HuIL-13 interact with the IL-4 receptor alpha (IL-4Rα) region and helix D is responsible for the interaction with the IL-13 receptor alpha 1 (IL-13Rα 1) receptor.

KW - Asthma

KW - Cytokine

KW - Homology modelling

KW - Interleukin-13

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U2 - 10.1046/j.1440-1711.2001.01035.x

DO - 10.1046/j.1440-1711.2001.01035.x

M3 - Article

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VL - 79

SP - 332

EP - 339

JO - Immunology and Cell Biology

JF - Immunology and Cell Biology

IS - 4

ER -

Structural model of human IL-13 defines the spatial interactions with the IL-13Rα/IL-4Rα receptor

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