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PDBsum entry 1gh7
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Cytokine receptor
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PDB id
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1gh7
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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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.
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Authors
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P.D.Carr,
S.E.Gustin,
A.P.Church,
J.M.Murphy,
S.C.Ford,
D.A.Mann,
D.M.Woltring,
I.Walker,
D.L.Ollis,
I.G.Young.
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Ref.
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Cell, 2001,
104,
291-300.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 3.
Figure 3. Structure of Domain 4The positions of the side
chains that form the Trp–Arg zipper and those of the
“affinity converting” residues are shown.
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Figure 6.
Figure 6. Surface Plots Produced by GRASP
([19])Orientations of the molecule are the same as in Figure 1.
Color coding: green, hydrophobic regions; and blue, polar
regions.
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2001,
104,
291-300)
copyright 2001.
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