Related ArticlesSecondary 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. Interaction of these cytokines with the IL-1 receptor induces a variety of biological changes in neurologic, metabolic, hematologic, and endocrinologic systems. Interleukin-1 receptor antagonist protein (IRAP) is a naturally occurring inhibitor of the interleukin-1 receptor. The 153-residue protein binds to the receptor with an affinity similar to that of IL-1 beta but does not elicit any physiological responses. As a first step toward understanding IRAP's mode of action, we have used multidimensional, heteronuclear NMR spectroscopy to determine the antagonist's solution secondary structure and global fold. Using a combination of 3D 1H-15N NOESY-HMQC and TOCSY-HMQC and 3D 1H-15N-13C HNCA and HN(CO)CA experiments on uniformly 15N- or doubly 13C/15N-enriched IRAP, we have made resonance assignments for more than 90% of the main-chain atoms. Analysis of short- and long-range NOE's indicates that IRAP is predominantly beta-sheet, with the same overall topology as IL-1 beta but with different regions of the primary sequence comprising the beta-strands. Two short helical segments also were identified. The 14% sequence identity between IL-1 beta and IRAP increases to 25% when differences in the locations of secondary structure elements in the primary sequences are taken into account. Still, numerous differences in side chains, which ultimately play a major role in receptor interaction, exist.(ABSTRACT TRUNCATED AT 250 WORDS)
[NMR paper] Solution secondary structure of a bacterially expressed peptide from the receptor bin
Solution secondary structure of a bacterially expressed peptide from the receptor binding domain of Pseudomonas aeruginosa pili strain PAK: A heteronuclear multidimensional NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution secondary structure of a bacterially expressed peptide from the receptor binding domain of Pseudomonas aeruginosa pili strain PAK: A heteronuclear multidimensional NMR study.
Biochemistry. 1997 Oct 21;36(42):12791-801
Authors: Campbell AP, Bautista DL, Tripet B,...
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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] Proton and nitrogen NMR sequence-specific assignments and secondary structure determi
Proton and nitrogen NMR sequence-specific assignments and secondary structure determination of the Bacillus subtilis SPO1-encoded transcription factor 1.
Related Articles Proton and nitrogen NMR sequence-specific assignments and secondary structure determination of the Bacillus subtilis SPO1-encoded transcription factor 1.
Biochemistry. 1994 Jul 26;33(29):8842-52
Authors: Jia X, Reisman JM, Hsu VL, Geiduschek EP, Parello J, Kearns DR
Sequence-specific 1H and 15N NMR1 assignments are reported for the transcription factor 1 (TF1), a 22-kDa type...
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[NMR paper] Proton NMR sequence-specific assignments and secondary structure of a receptor bindin
Proton NMR sequence-specific assignments and secondary structure of a receptor binding domain of mouse gamma-interferon.
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Biochemistry. 1993 Jun 1;32(21):5650-5
Authors: Sakai TT, Jablonsky MJ, DeMuth PA, Krishna NR, Jarpe MA, Johnson HM
Previous studies using synthetic peptides and monoclonal antibodies have implicated the N-terminal 39-residue segment as a receptor binding region of mouse gamma-interferon...
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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.
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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] 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...