1il6

From Proteopedia

Revision as of 14:02, 15 February 2008

HUMAN INTERLEUKIN-6, NMR, MINIMIZED AVERAGE STRUCTURE

Overview

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.

Disease

Known diseases associated with this structure: Kaposi sarcoma, susceptibility to OMIM:[147620], Osteopenia/osteoporosis OMIM:[147620]

About this Structure

1IL6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Solution structure of recombinant human interleukin-6., Xu GY, Yu HA, Hong J, Stahl M, McDonagh T, Kay LE, Cumming DA, J Mol Biol. 1997 May 2;268(2):468-81. PMID:9159484

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