Crystal Structure of the Interleukin-4/Receptor α Chain Complex Reveals a Mosaic Binding Interface
Copyright policy )Crystal Structure of the Interleukin-4/Receptor α Chain Complex Reveals a Mosaic Binding Interface
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.
- University of Würzburg Germany
- Bayer (Germany) Germany
- Bayer Germany
Models, Molecular, Binding Sites, Sequence Homology, Amino Acid, Biochemistry, Genetics and Molecular Biology(all), Macromolecular Substances, Protein Conformation, Molecular Sequence Data, In Vitro Techniques, Crystallography, X-Ray, Receptors, Interleukin-4, Humans, Amino Acid Sequence, Interleukin-4, Receptors, Cytokine, Signal Transduction
Models, Molecular, Binding Sites, Sequence Homology, Amino Acid, Biochemistry, Genetics and Molecular Biology(all), Macromolecular Substances, Protein Conformation, Molecular Sequence Data, In Vitro Techniques, Crystallography, X-Ray, Receptors, Interleukin-4, Humans, Amino Acid Sequence, Interleukin-4, Receptors, Cytokine, Signal Transduction
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