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Structure. 2010 May 12;18(5):638-48. doi: 10.1016/j.str.2010.02.009.

Structure and mechanism of receptor sharing by the IL-10R2 common chain.

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  • 1Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.

Abstract

IL-10R2 is a shared cell surface receptor required for the activation of five class 2 cytokines (IL-10, IL-22, IL-26, IL-28, and IL-29) that play critical roles in host defense. To define the molecular mechanisms that regulate its promiscuous binding, we have determined the crystal structure of the IL-10R2 ectodomain at 2.14 A resolution. IL-10R2 residues required for binding were identified by alanine scanning and used to derive computational models of IL-10/IL-10R1/IL-10R2 and IL-22/IL-22R1/IL-10R2 ternary complexes. The models reveal a conserved binding epitope that is surrounded by two clefts that accommodate the structural and chemical diversity of the cytokines. These results provide a structural framework for interpreting IL-10R2 single nucleotide polymorphisms associated with human disease.

Copyright 2010 Elsevier Ltd. All rights reserved.

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PMID:
20462497
[PubMed - indexed for MEDLINE]
PMCID:
PMC2879597
Free PMC Article
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