Structural highlights
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 PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
Contents | ||||||||||||||||
This page was last modified 04:45, 29 September 2014.