The structural basis for receptor recognition of human interleukin-18
Copyright policy )The structural basis for receptor recognition of human interleukin-18
AbstractInterleukin (IL)-18 is a proinflammatory cytokine that belongs to the IL-1 family and plays an important role in inflammation. The uncontrolled release of this cytokine is associated with severe chronic inflammatory disease. IL-18 forms a signalling complex with the IL-18 receptor α (Rα) and β (Rβ) chains at the plasma membrane, which induces multiple inflammatory cytokines. Here, we present a crystal structure of human IL-18 bound to the two receptor extracellular domains. Generally, the receptors’ recognition mode for IL-18 is similar to IL-1β; however, certain notable differences were observed. The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode. The structures and associated biochemical and cellular data should aid in developing novel drugs to neutralize IL-18 activity.
- Kyoto University Japan
- Heisei College of Health Sciences Japan
- Argonne National Laboratory United States
- Hokkaido Bunkyo University Japan
- Yokohama City University Japan
Immunology, Interleukin-1beta, Molecular Sequence Data, Gene Expression, Crystallography, X-Ray, Biochemistry, Article, Protein Structure, Secondary, Animals, Humans, Amino Acid Sequence, Receptors, Interleukin-18, Binding Sites, Sequence Homology, Amino Acid, Interleukin-18, Receptors, Interleukin, Recombinant Proteins, Protein Structure, Tertiary, Biological sciences, Protein Subunits, Mutation, Interleukin-1 Receptor Accessory Protein, Baculoviridae, Protein Binding
Immunology, Interleukin-1beta, Molecular Sequence Data, Gene Expression, Crystallography, X-Ray, Biochemistry, Article, Protein Structure, Secondary, Animals, Humans, Amino Acid Sequence, Receptors, Interleukin-18, Binding Sites, Sequence Homology, Amino Acid, Interleukin-18, Receptors, Interleukin, Recombinant Proteins, Protein Structure, Tertiary, Biological sciences, Protein Subunits, Mutation, Interleukin-1 Receptor Accessory Protein, Baculoviridae, Protein Binding
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