Related ArticlesDetermination of the secondary structure and molecular topology of interleukin-1 beta by use of two- and three-dimensional heteronuclear 15N-1H NMR spectroscopy.
A study of the regular secondary structure elements of recombinant human interleukin-1 beta has been carried out using NMR spectroscopy. Using a randomly 15N labeled sample, a number of heteronuclear three- and two-dimensional NMR experiments have been performed, which have enabled a complete analysis of short-, medium-, and long-range NOEs between protons of the polypeptide backbone, based on the sequence-specific resonance assignments that have been reported previously [Driscoll, P. C., Clore, G. M., Marion, D., Wingfield, P. T., & Gronenborn, A. M. (1990) Biochemistry 29, 3542-3556]. In addition, accurate measurements of a large number of 3JHN alpha coupling constants have been carried out by two-dimensional heteronuclear multiple-quantum-coherence-J spectroscopy. Amide NH solvent exchange rates have been measured by following the time dependence of the 15N-1H correlation spectrum of interleukin-1 beta on dissolving the protein in D2O solution. Analysis of these data indicate that the structure of interleukin-1 beta consists of 12 extended beta-strands aligned in a single extended network of antiparallel beta-sheet structure that in part folds into a skewed six-stranded beta-barrel. In the overall structure the beta-strands are connected by tight turns, short loops, and long loops in a manner that displays approximate pseudo-three-fold symmetry. The secondary structure analysis is discussed in the light of the unrefined X-ray structure of interleukin-1 beta at 3-A resolution [Priestle, J. P., Schär, H.-P., & Grütter, M. G. (1988) EMBO J. 7, 339-343], as well as biological activity data. Discernible differences between the two studies are highlighted. Finally, we have discovered conformational heterogeneity in the structure of interleukin-1 beta, which is characterized by an exchange rate that is slow on the NMR chemical shift time scale.
[NMR paper] Direct determination of the interleukin-6 binding epitope of the interleukin-6 recept
Direct determination of the interleukin-6 binding epitope of the interleukin-6 receptor by NMR spectroscopy.
Related Articles Direct determination of the interleukin-6 binding epitope of the interleukin-6 receptor by NMR spectroscopy.
J Biol Chem. 2004 Jan 2;279(1):571-6
Authors: Schwantner A, Dingley AJ, Ozbek S, Rose-John S, Grötzinger J
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...
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[NMR paper] 1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Esch
1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Escherichia coli GlgS protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Escherichia coli GlgS protein.
Eur J Biochem. 1997 Jun 1;246(2):301-10
Authors: Beglova N, Fischer D, Hengge-Aronis R, Gehring K
GlgS is a 7892-Da protein which is involved in glycogen...
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[NMR paper] 1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Esch
1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Escherichia coli GlgS protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Escherichia coli GlgS protein.
Eur J Biochem. 1997 Jun 1;246(2):301-10
Authors: Beglova N, Fischer D, Hengge-Aronis R, Gehring K
GlgS is a 7892-Da protein which is involved in glycogen...
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[NMR paper] 1H resonance assignments, secondary structure and general topology of single-chain mo
1H resonance assignments, secondary structure and general topology of single-chain monellin in solution as determined by 1H 2D-NMR.
Related Articles 1H resonance assignments, secondary structure and general topology of single-chain monellin in solution as determined by 1H 2D-NMR.
J Biomol NMR. 1992 Nov;2(6):557-72
Authors: Tomic MT, Somoza JR, Wemmer DE, Park YW, Cho JM, Kim SH
We determined the resonance assignments, secondary structure and general topology of the 11-kDa sweet protein single-chain monellin (SCM), using two-dimensional proton...
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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] 1H NMR identification of a beta-sheet structure and description of folding topology i
1H NMR identification of a beta-sheet structure and description of folding topology in putidaredoxin.
Related Articles 1H NMR identification of a beta-sheet structure and description of folding topology in putidaredoxin.
Biochemistry. 1991 Apr 23;30(16):3850-6
Authors: Pochapsky TC, Ye XM
Putidaredoxin (Pdx), a 106-residue globular protein consisting of a single polypeptide chain and a cluster, is the physiological reductant of P-450cam, which in turn catalyzes the monohydroxylation of camphor by molecular oxygen. No crystal structure has...
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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...
Determination of the secondary structure and molecular topology of interleukin-1 beta
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