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PMID:10219247

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Citation

Hage, T, Sebald, W and Reinemer, P (1999) Crystal structure of the interleukin-4/receptor alpha chain complex reveals a mosaic binding interface. Cell 97:271-81

Abstract

Interleukin-4 (IL-4) is a principal regulatory cytokine during an immune response and a crucial determinant for allergy and asthma. IL-4 binds with high affinity and specificity to the ectodomain of the IL-4 receptor alpha chain (IL4-BP). Subsequently, this intermediate complex recruits the common gamma chain (gamma c), thereby initiating transmembrane signaling. The crystal structure of the intermediate complex between human IL-4 and IL4-BP was determined at 2.3 A resolution. It reveals a novel spatial orientation of the two proteins, a small but unexpected conformational change in the receptor-bound IL-4, and an interface with three separate clusters of trans-interacting residues. Novel insights on ligand binding in the cytokine receptor family and a paradigm for receptors of IL-2, IL-7, IL-9, and IL-15, which all utilize gamma c, are provided.

Links

PubMed

Keywords

Amino Acid Sequence; Binding Sites; Crystallography, X-Ray; Humans; Interleukin-4/chemistry; Interleukin-4/metabolism; Macromolecular Substances; Models, Molecular; Molecular Sequence Data; Protein Conformation; Receptors, Cytokine/chemistry; Receptors, Cytokine/genetics; Receptors, Interleukin-4/chemistry; Receptors, Interleukin-4/genetics; Receptors, Interleukin-4/metabolism; Sequence Homology, Amino Acid; Signal Transduction

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:IL4

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P24394

F

Seeded From UniProt

complete

HUMAN:IL4RA

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P05112

F

Seeded From UniProt

complete


See also

References

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