PDBsum entry: 2il6

Cytokine

PDB id: 2il6

Contents

Protein chain

166 a.a. *

* Residue conservation analysis

PDB id:

2il6

Name:

Cytokine

Title:

Human interleukin-6, nmr, 32 structures

Structure:

Interleukin-6. Chain: a. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562

NMR struc:

32 models

Authors:

G.Y.Xu,H.A.Yu,J.Hong,M.Stahl,T.Mcdonagh,L.E.Kay,D.A.Cumming

Key ref:

G.Y.Xu et al. (1997). Solution structure of recombinant human interleukin-6. J Mol Biol, 268, 468-481. PubMed id: 9159484 DOI: 10.1006/jmbi.1997.0933

Date:

31-Jan-97 Release date: 04-Feb-98

Protein chain

P05231  (IL6_HUMAN) -  Interleukin-6

Seq: 212 a.a.

Struc: 166 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: extracellular region (1 term)
• Biological process: immune response (1 term)
• Biochemical function: cytokine activity (2 terms)

DOI no: 10.1006/jmbi.1997.0933

J Mol Biol 268:468-481 (1997)

PubMed id: 9159484

Solution structure of recombinant human interleukin-6.

G.Y.Xu, H.A.Yu, J.Hong, M.Stahl, T.McDonagh, L.E.Kay, D.A.Cumming.

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.

Selected figure(s)

Figure 3.
Figure 3. Stereo image of the averaged and minimized NMR structure of IL-6. Only residues 20 to 185 are shown and individual helices are labeled.

Figure 4.
Figure 4. Best-fit superposition of the C^α atoms of the X-ray and the restrained minimized averaged NMR structures of IL-6. (a) The color coding scheme is identical to that of Figure 1. The average minimized NMR structure is shown in thick lines while the X-ray structure is shown in thin lines. (b) C^α-C^α distances after the best-fit superposition.

The above figures are reprinted by permission from Elsevier: J Mol Biol (1997, 268, 468-481) copyright 1997.

Figures were selected by an automated process.