1n26

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spinqualitylabelsall models 1n26, resolution 2.4Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of the extra-cellular domains of Human Interleukin-6 Receptor alpha chain

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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