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1N26

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

Summary for 1N26
Entry DOI10.2210/pdb1n26/pdb
Related1I1R 1IL6 1N2Q
DescriptorIL-6 Receptor alpha chain, 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
Functional Keywordstransmembrane, glycoprotein, immunoglobulin domain, cytokine
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight38541.88
Authors
Varghese, J.N.,Moritz, R.L.,Lou, M.-Z.,van Donkelaar, A.,Ji, H.,Ivancic, N.,Branson, K.M.,Hall, N.E.,Simpson, R.J. (deposition date: 2002-10-22, release date: 2002-12-18, Last modification date: 2024-11-20)
Primary citationVarghese, J.N.,Moritz, R.L.,Lou, M.-Z.,van Donkelaar, A.,Ji, H.,Ivancic, N.,Branson, K.M.,Hall, N.E.,Simpson, R.J.
Structure of the extracellular domains of the human interleukin-6 receptor alpha-chain.
Proc.Natl.Acad.Sci.USA, 99:15959-15964, 2002
Cited by
PubMed Abstract: 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.
PubMed: 12461182
DOI: 10.1073/pnas.232432399
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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