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2IL6

HUMAN INTERLEUKIN-6, NMR, 32 STRUCTURES

Summary for 2IL6
Entry DOI10.2210/pdb2il6/pdb
DescriptorINTERLEUKIN-6 (1 entity in total)
Functional Keywordscytokine, glycoprotein, growth factor
Biological sourceHomo sapiens (human)
Cellular locationSecreted: P05231
Total number of polymer chains1
Total formula weight21005.96
Authors
Xu, G.Y.,Yu, H.A.,Hong, J.,Stahl, M.,Mcdonagh, T.,Kay, L.E.,Cumming, D.A. (deposition date: 1997-01-31, release date: 1998-02-04, Last modification date: 2022-03-09)
Primary citationXu, G.Y.,Yu, H.A.,Hong, J.,Stahl, M.,McDonagh, T.,Kay, L.E.,Cumming, D.A.
Solution structure of recombinant human interleukin-6.
J.Mol.Biol., 268:468-481, 1997
Cited by
PubMed Abstract: Interleukin-6 (IL-6) is a 185 amino acid cytokine which exerts multiple biological effects in vivo and whose dysregulation underlies several disease processes. The solution structure of recombinant human interleukin-6 has now been determined using heteronuclear three and four-dimensional NMR spectroscopy. The structure of the molecule was determined using 3044 distance and torsion restraints derived by NMR spectroscopy to generate an ensemble of 32 structures using a combined distance geometry/simulated annealing protocol. The protein contains five alpha-helices interspersed with variable-length loops; four of these helices constitute a classical four-helix bundle with the fifth helix located in the CD loop. There were no distance violations greater than 0.3 A in any of the final 32 structures and the ensemble has an average-to-the-mean backbone root-mean-square deviation of 0.50 A for the core four-helix bundle. Although the amino-terminal 19 amino acids are disordered in solution, the remainder of the molecule has a well defined structure that shares many features displayed by other long-chain four-helix bundle cytokines. The high-resolution NMR structure of hIL-6 is used to rationalize available mutagenesis data in terms of a heteromeric receptor complex.
PubMed: 9159484
DOI: 10.1006/jmbi.1997.0933
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

226707

數據於2024-10-30公開中

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