1n26 | pdb_00001n26
Crystal Structure of the extra-cellular domains of Human Interleukin-6 Receptor alpha chain
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Overview
Dysregulated production of IL-6 and its receptor (IL-6R) are implicated in the pathogenesis of multiple myeloma, autoimmune diseases and prostate cancer. The IL-6R complex comprises two molecules each of IL-6, IL-6R, and the signaling molecule, gp130. Here, we report the x-ray structure (2.4 A) of the IL-6R ectodomains. The N-terminal strand of the Ig-like domain (D(1)) is disulfide-bonded to domain D(2), and domains D(2) and D(3), the cytokine-binding domain, are structurally similar to known cytokine-binding domains. The head-to-tail packing of two closely associated IL-6R molecules observed in the crystal may be representative of the configuration of the physiological dimer of IL-6R and provides new insight into the architecture of the IL-6R complex.
About this Structure
1N26 is a Single protein structure of sequence from Homo sapiens with NAG, SO4 and CYS as ligands. Full crystallographic information is available from OCA.
Reference
Structure of the extracellular domains of the human interleukin-6 receptor alpha -chain., Varghese JN, Moritz RL, Lou MZ, Van Donkelaar A, Ji H, Ivancic N, Branson KM, Hall NE, Simpson RJ, Proc Natl Acad Sci U S A. 2002 Dec 10;99(25):15959-64. Epub 2002 Dec 2. PMID:12461182
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