Structure of the Complete Extracellular Domain of the Common β Subunit of the Human GM-CSF, IL-3, and IL-5 Receptors Reveals a Novel Dimer Configuration
| Autor: | David L. Ollis, Paul D. Carr, Ian Walker, Alice P. Church, David A. Mann, Donna Woltring, Ian G. Young, James M. Murphy, Sonja E. Gustin, Sally C. Ford |
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| Rok vydání: | 2001 |
| Předmět: |
Models
Molecular Protein Folding Protein Conformation Blotting Western Molecular Sequence Data Beta sheet Interleukin-17 receptor Biology Ligands General Biochemistry Genetics and Molecular Biology Interleukin 10 receptor alpha subunit Protein structure Animals Humans Amino Acid Sequence Protein Structure Quaternary Common gamma chain Biochemistry Genetics and Molecular Biology(all) Receptors Interleukin Interleukin-13 receptor Glycoprotein 130 Receptors Interleukin-5 Receptors Interleukin-3 Cell biology Protein Structure Tertiary Protein Subunits Biochemistry Receptors Granulocyte-Macrophage Colony-Stimulating Factor Cytokine receptor Baculoviridae Dimerization Sequence Alignment Protein Binding |
| Zdroj: | Cell. 104(2):291-300 |
| ISSN: | 0092-8674 |
| DOI: | 10.1016/s0092-8674(01)00213-6 |
| Popis: | The receptor systems for the hemopoietic cytokines GM-CSF, IL-3, and IL-5 consist of ligand-specific alpha receptor subunits that play an essential role in the activation of the shared betac subunit, the major signaling entity. Here, we report the structure of the complete betac extracellular domain. It has a structure unlike any class I cytokine receptor described thus far, forming a stable interlocking dimer in the absence of ligand in which the G strand of domain 1 hydrogen bonds into the corresponding beta sheet of domain 3 of the dimer-related molecule. The G strand of domain 3 similarly partners with the dimer-related domain 1. The structure provides new insights into receptor activation by the respective alpha receptor:ligand complexes. |
| Databáze: | OpenAIRE |
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