Homodimeric cross-over structure of the human granulocyte colony-stimulating factor (GCSF) receptor signaling complex
Copyright policy )Homodimeric cross-over structure of the human granulocyte colony-stimulating factor (GCSF) receptor signaling complex
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 Å 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.
- Kagoshima University Japan
- Japan Atomic Energy Agency Japan
Models, Molecular, Binding Sites, Molecular Sequence Data, Crystallography, X-Ray, Ligands, Recombinant Proteins, Structural Homology, Protein, Granulocyte Colony-Stimulating Factor, Receptors, Granulocyte Colony-Stimulating Factor, Cytokine Receptor gp130, Humans, Amino Acid Sequence, Protein Structure, Quaternary, Dimerization, Sequence Alignment, Conserved Sequence, Signal Transduction
Models, Molecular, Binding Sites, Molecular Sequence Data, Crystallography, X-Ray, Ligands, Recombinant Proteins, Structural Homology, Protein, Granulocyte Colony-Stimulating Factor, Receptors, Granulocyte Colony-Stimulating Factor, Cytokine Receptor gp130, Humans, Amino Acid Sequence, Protein Structure, Quaternary, Dimerization, Sequence Alignment, Conserved Sequence, Signal Transduction
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