2ARW
The solution structure of the membrane proximal cytokine receptor domain of the human interleukin-6 receptor
Summary for 2ARW
Entry DOI | 10.2210/pdb2arw/pdb |
NMR Information | BMRB: 5940 |
Descriptor | Interleukin-6 receptor alpha chain (1 entity in total) |
Functional Keywords | fibronectin-type iii like, cytokine |
Biological source | Homo sapiens (human) |
Total number of polymer chains | 1 |
Total formula weight | 14680.38 |
Authors | Hecht, O.,Dingley, A.J.,Schwantner, A.,Ozbek, S.,Rose-John, S.,Grotzinger, J. (deposition date: 2005-08-22, release date: 2006-09-12, Last modification date: 2024-05-01) |
Primary citation | Hecht, O.,Dingley, A.J.,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., 387:1255-1259, 2006 Cited by PubMed Abstract: 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. PubMed: 16972794DOI: 10.1515/BC.2006.155 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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