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1GH7

CRYSTAL STRUCTURE OF THE COMPLETE EXTRACELLULAR DOMAIN OF THE BETA-COMMON RECEPTOR OF IL-3, IL-5, AND GM-CSF

Summary for 1GH7
Entry DOI10.2210/pdb1gh7/pdb
DescriptorCYTOKINE RECEPTOR COMMON BETA CHAIN, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
Functional Keywordsdimer of interlocking chains of fibronectin-iii domains four fibronectin-iii domains per chain, cytokine receptor
Biological sourceHomo sapiens (human)
Total number of polymer chains2
Total formula weight97939.11
Authors
Carr, P.D.,Gustin, S.E.,Church, A.P.,Murphy, J.M.,Ford, S.C.,Mann, D.A.,Woltring, D.M.,Walker, I.,Ollis, D.L.,Young, I.G. (deposition date: 2000-11-27, release date: 2001-11-28, Last modification date: 2024-11-13)
Primary citationCarr, P.D.,Gustin, S.E.,Church, A.P.,Murphy, J.M.,Ford, S.C.,Mann, D.A.,Woltring, D.M.,Walker, I.,Ollis, D.L.,Young, I.G.
Structure of the complete extracellular domain of the common beta subunit of the human GM-CSF, IL-3, and IL-5 receptors reveals a novel dimer configuration.
Cell(Cambridge,Mass.), 104:291-300, 2001
Cited by
PubMed Abstract: 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.
PubMed: 11207369
DOI: 10.1016/S0092-8674(01)00213-6
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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