Abstract
A crystal structure of the signaling complex between human granulocyte colony-stimulating factor (GCSF) and a ligand binding region of GCSF receptor (GCSF-R), has been determined to 2.8 A resolution. The GCSF:GCSF-R complex formed a 2:2 stoichiometry by means of a cross-over interaction between the Ig-like domains of GCSF-R and GCSF. The conformation of the complex is quite different from that between human GCSF and the cytokine receptor homologous domain of mouse GCSF-R, but similar to that of the IL-6/gp130 signaling complex. The Ig-like domain cross-over structure necessary for GCSF-R activation is consistent with previously reported thermodynamic and mutational analyses.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Conserved Sequence
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Crystallography, X-Ray
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Cytokine Receptor gp130 / chemistry
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Cytokine Receptor gp130 / metabolism
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Dimerization
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Granulocyte Colony-Stimulating Factor / chemistry*
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Granulocyte Colony-Stimulating Factor / genetics
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Granulocyte Colony-Stimulating Factor / metabolism*
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Humans
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Ligands
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Models, Molecular
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Molecular Sequence Data
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Protein Structure, Quaternary
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Receptors, Granulocyte Colony-Stimulating Factor / chemistry*
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Receptors, Granulocyte Colony-Stimulating Factor / genetics
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Receptors, Granulocyte Colony-Stimulating Factor / metabolism*
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Recombinant Proteins
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Sequence Alignment
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Signal Transduction*
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Structural Homology, Protein
Substances
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Ligands
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Receptors, Granulocyte Colony-Stimulating Factor
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Recombinant Proteins
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Cytokine Receptor gp130
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Granulocyte Colony-Stimulating Factor