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2d9q

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|PDB= 2d9q |SIZE=350|CAPTION= <scene name='initialview01'>2d9q</scene>, resolution 2.80&Aring;
|PDB= 2d9q |SIZE=350|CAPTION= <scene name='initialview01'>2d9q</scene>, resolution 2.80&Aring;
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d9q OCA], [http://www.ebi.ac.uk/pdbsum/2d9q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d9q RCSB]</span>
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[[Category: ligand-receptor complex]]
[[Category: ligand-receptor complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:24:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:31:47 2008''

Revision as of 23:31, 30 March 2008


PDB ID 2d9q

Drag the structure with the mouse to rotate
, resolution 2.80Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the Human GCSF-Receptor Signaling Complex


Overview

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.

About this Structure

2D9Q is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Homodimeric cross-over structure of the human granulocyte colony-stimulating factor (GCSF) receptor signaling complex., Tamada T, Honjo E, Maeda Y, Okamoto T, Ishibashi M, Tokunaga M, Kuroki R, Proc Natl Acad Sci U S A. 2006 Feb 28;103(9):3135-40. Epub 2006 Feb 21. PMID:16492764

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