1il6

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==Overview==
==Overview==
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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.
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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==
==Disease==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Cumming, D.A.]]
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[[Category: Cumming, D A.]]
[[Category: Hong, J.]]
[[Category: Hong, J.]]
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[[Category: Kay, L.E.]]
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[[Category: Kay, L E.]]
[[Category: Mcdonagh, T.]]
[[Category: Mcdonagh, T.]]
[[Category: Stahl, M.]]
[[Category: Stahl, M.]]
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[[Category: Xu, G.Y.]]
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[[Category: Xu, G Y.]]
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[[Category: Yu, H.A.]]
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[[Category: Yu, H A.]]
[[Category: cytokine]]
[[Category: cytokine]]
[[Category: glycoprotein]]
[[Category: glycoprotein]]
[[Category: growth factor]]
[[Category: growth factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:02:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:02 2008''

Revision as of 11:13, 21 February 2008

Image:1il6.jpg

1il6

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HUMAN INTERLEUKIN-6, NMR, MINIMIZED AVERAGE STRUCTURE

Contents

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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