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2arw

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The solution structure of the membrane proximal cytokine receptor domain of the human interleukin-6 receptorThe solution structure of the membrane proximal cytokine receptor domain of the human interleukin-6 receptor

Structural highlights

2arw is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[IL6RA_HUMAN] Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal. Signal activation necessitate an association with IL6ST. Activation may lead to the regulation of the immune response, acute-phase reactions and hematopoiesis.[1] [2] Low concentration of a soluble form of IL6 receptor acts as an agonist of IL6 activity.[3] [4]

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

The solution structure of the membrane-proximal cytokine receptor domain of the human interleukin-6 receptor.,Hecht O, Dingley AJ, Schwanter A, Ozbek S, Rose-John S, Grotzinger J Biol Chem. 2006 Sep;387(9):1255-9. PMID:16972794[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Martens AS, Bode JG, Heinrich PC, Graeve L. The cytoplasmic domain of the interleukin-6 receptor gp80 mediates its basolateral sorting in polarized madin-darby canine kidney cells. J Cell Sci. 2000 Oct;113 ( Pt 20):3593-602. PMID:11017875
  2. ↑ Buk DM, Renner O, Graeve L. Increased association with detergent-resistant membranes/lipid rafts of apically targeted mutants of the interleukin-6 receptor gp80. Eur J Cell Biol. 2005 Oct;84(10):819-31. PMID:16270750
  3. ↑ Martens AS, Bode JG, Heinrich PC, Graeve L. The cytoplasmic domain of the interleukin-6 receptor gp80 mediates its basolateral sorting in polarized madin-darby canine kidney cells. J Cell Sci. 2000 Oct;113 ( Pt 20):3593-602. PMID:11017875
  4. ↑ Buk DM, Renner O, Graeve L. Increased association with detergent-resistant membranes/lipid rafts of apically targeted mutants of the interleukin-6 receptor gp80. Eur J Cell Biol. 2005 Oct;84(10):819-31. PMID:16270750
  5. ↑ Hecht O, Dingley AJ, Schwanter A, Ozbek S, Rose-John S, Grotzinger J. The solution structure of the membrane-proximal cytokine receptor domain of the human interleukin-6 receptor. Biol Chem. 2006 Sep;387(9):1255-9. PMID:16972794 doi:10.1515/BC.2006.155
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