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Homodimeric cross-over structure of the human granulocyte colony-stimulating factor (GCSF) receptor signaling complex.


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.

SUBMITTER: Tamada T 

PROVIDER: S-EPMC1413920 | biostudies-literature | 2006 Feb

REPOSITORIES: biostudies-literature

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Homodimeric cross-over structure of the human granulocyte colony-stimulating factor (GCSF) receptor signaling complex.

Tamada Taro T   Honjo Eijiro E   Maeda Yoshitake Y   Okamoto Tomoyuki T   Ishibashi Matsujiro M   Tokunaga Masao M   Kuroki Ryota R  

Proceedings of the National Academy of Sciences of the United States of America 20060221 9


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  ...[more]

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