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PDBsum entry 2arw
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References listed in PDB file
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Key reference
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Title
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The solution structure of the membrane-Proximal cytokine receptor domain of the human interleukin-6 receptor.
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Authors
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O.Hecht,
A.J.Dingley,
A.Schwanter,
S.Ozbek,
S.Rose-John,
J.Grötzinger.
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Ref.
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Biol Chem, 2006,
387,
1255-1259.
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PubMed id
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Abstract
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The members of the interleukin-6-type family of cytokines interact with
receptors that have a modular structure and are built of several
immunoglobulin-like and fibronectin type III-like domains. These receptors have
a characteristic cytokine receptor homology region consisting of two fibronectin
type III-like domains defined by a set of four conserved cysteines and a
tryptophan-serine-X-tryptophan-serine sequence motif. On target cells,
interleukin-6 (IL-6) initially binds to its cognate alpha-receptor and
subsequently to a homodimer of the signal transducer receptor gp130. The IL-6
receptor (IL-6R) consists of three extracellular domains. The N-terminal
immunoglobulin-like domain is not involved in ligand binding, whereas the third
membrane-proximal fibronectin-like domain (IL-6R-D3) accounts for more than 90%
of the binding energy to IL-6. Here, we present the solution structure of the
IL-6R-D3 domain solved by multidimensional heteronuclear NMR spectroscopy.
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