All cytokines belonging to the interleukin-6 (IL-6)-type family of cytokines utilize receptors that have a modular build of several immunoglobulin-like and fibronectin type III-like domains. Characteristic of these receptors is a cytokine receptor homology region consisting of two such fibronectin domains defined by a set of four conserved cysteines and a tryptophan-serine-X-tryptophan-serine sequence motif. On target cells, interleukin-6 first binds to its specific receptor and subsequently to a homodimer of the signal transducer protein gp130. The interleukin-6 receptor consists of three extracellular domains. The N-terminal immunoglobulin-like domain is not involved in ligand binding, whereas the third membrane proximal fibronectin-like domain accounts for more than 90% of the binding energy to IL-6. Here, the key residues of this fibronectin-like domain involved in the interaction with IL-6 are described. Chemical shift mapping data with 15N-labeled IL-6R-D3 and unlabeled IL-6 coupled with recent structural data clearly reveal the epitope within the IL-6R-D3 responsible for mediating the high affinity interaction with its cognate cytokine.
[NMR paper] NMR studies of the solution properties of recombinant murine interleukin-6.
NMR studies of the solution properties of recombinant murine interleukin-6.
Related Articles NMR studies of the solution properties of recombinant murine interleukin-6.
Biochim Biophys Acta. 1995 Jun 12;1249(2):189-203
Authors: Morton CJ, Bai H, Zhang JG, Hammacher A, Norton RS, Simpson RJ, Mabbutt BC
The effects of solvent, pH and temperature on the 1H-NMR spectra of recombinant murine interleukin-6 (IL-6) are described. Assignments made from two-dimensional homonuclear spectra are presented for resonances of the fifteen aromatic amino-acid...
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[NMR paper] Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments.
Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments.
Related Articles Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments.
Biochemistry. 1992 Aug 25;31(33):7741-4
Authors: Mott HR, Driscoll PC, Boyd J, Cooke RM, Weir MP, Campbell ID
Recombinant 15N-labeled human interleukin 2 (IL-2) has been studied by 2D and 3D NMR using uniformly 15N-labeled protein. Assignment of the backbone resonances has enabled the secondary structure of the protein to be defined. The secondary structure was...
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[NMR paper] Secondary structure and topology of interleukin-1 receptor antagonist protein determi
Secondary structure and topology of interleukin-1 receptor antagonist protein determined by heteronuclear three-dimensional NMR spectroscopy.
Related Articles Secondary structure and topology of interleukin-1 receptor antagonist protein determined by heteronuclear three-dimensional NMR spectroscopy.
Biochemistry. 1992 Jun 16;31(23):5237-45
Authors: Stockman BJ, Scahill TA, Roy M, Ulrich EL, Strakalaitis NA, Brunner DP, Yem AW, Deibel MR
Interleukin-1 (IL-1) proteins, such as IL-1 beta, play a key role in immune and inflammatory responses....
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[NMR paper] Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double
Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy.
Related Articles Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy.
Biochemistry. 1990 Sep 4;29(35):8172-84
Authors: Clore GM, Bax A, Driscoll PC, Wingfield PT, Gronenborn AM
The assignment of the aliphatic 1H and 13C resonances of IL-1 beta, a protein of 153 residues and molecular...
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[NMR paper] Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse
Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy.
Related Articles Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy.
Biochemistry. 1990 Aug 14;29(32):7387-401
Authors: Clore GM, Driscoll PC, Wingfield PT, Gronenborn AM
The backbone dynamics of uniformly 15N-labeled interleukin-1 beta are investigated by using two-dimensional inverse detected heteronuclear 15N-1H NMR...
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[NMR paper] Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 bet
Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 beta in solution.
Related Articles Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 beta in solution.
Science. 1990 Jul 27;249(4967):411-4
Authors: Kay LE, Clore GM, Bax A, Gronenborn AM
A method is presented that dramatically improves the resolution of protein nuclear magnetic resonance (NMR) spectra by increasing their dimensionality to four. The power of this technique is demonstrated by the application of four-dimensional...
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[NMR paper] Determination of the secondary structure and molecular topology of interleukin-1 beta
Determination of the secondary structure and molecular topology of interleukin-1 beta by use of two- and three-dimensional heteronuclear 15N-1H NMR spectroscopy.
Related Articles Determination of the secondary structure and molecular topology of interleukin-1 beta by use of two- and three-dimensional heteronuclear 15N-1H NMR spectroscopy.
Biochemistry. 1990 May 15;29(19):4668-82
Authors: Driscoll PC, Gronenborn AM, Wingfield PT, Clore GM
A study of the regular secondary structure elements of recombinant human interleukin-1 beta has been...
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[NMR paper] Complete resonance assignment for the polypeptide backbone of interleukin 1 beta usin
Complete resonance assignment for the polypeptide backbone of interleukin 1 beta using three-dimensional heteronuclear NMR spectroscopy.
Related Articles Complete resonance assignment for the polypeptide backbone of interleukin 1 beta using three-dimensional heteronuclear NMR spectroscopy.
Biochemistry. 1990 Apr 10;29(14):3542-56
Authors: Driscoll PC, Clore GM, Marion D, Wingfield PT, Gronenborn AM
The complete sequence-specific assignment of the 15N and 1H backbone resonances of the NMR spectrum of recombinant human interleukin 1 beta (153...