Interferons are cytokines that play a complex role in the resistance of mammalian hosts to pathogens. IFNgamma (interferon-gamma) is secreted by activated T-cells and natural killer cells. IFNgamma is involved in a wide range of physiological processes, including antiviral activity, immune response, cell proliferation and apoptosis, as well as the stimulation and repression of a variety of genes. IFNgamma activity is modulated by the binding of its C-terminal domain to HS (heparan sulphate), a glycosaminoglycan found in the extracellular matrix and at the cell surface. In the present study, we analysed the interaction of isolated heparin-derived oligosaccharides with the C-terminal peptide of IFNgamma by NMR, in aqueous solution. We observed marked changes in the chemical shifts of both peptide and oligosaccharide compared with the free state. Our results provide evidence of a binding through electrostatic interactions between the charged side chains of the protein and the sulphate groups of heparin that does not induce specific conformation of the C-terminal part of IFNgamma. Our data also indicate that an oligosaccharide size of at least eight residues displays the most efficient binding.
[NMR paper] Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR an
Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy.
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Biochemistry. 2004 Aug 17;43(32):10393-9
Authors: Lysek DA, Wüthrich K
Transmissible spongiform encephalopathies have been observed exclusively in organisms expressing the host-encoded prion protein (PrP). The function of the cellular isoform of PrP found in healthy organisms has so far not been identified,...
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[NMR paper] NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with
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J Biol Chem. 2004 Jul 23;279(30):31455-61
Authors: Okubo S, Hara F, Tsuchida Y, Shimotakahara S, Suzuki S, Hatanaka H, Yokoyama S, Tanaka H, Yasuda H, Shindo H
A member of the PIAS (protein inhibitor of activated STAT) family of proteins, PIAS1, have been reported...
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[NMR paper] NMR structural characterization of the N-terminal domain of the adenylyl cyclase-asso
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J Biomol NMR. 2004 May;29(1):73-84
Authors: Mavoungou C, Israel L, Rehm T, Ksiazek D, Krajewski M, Popowicz G, Noegel AA, Schleicher M, Holak TA
Cyclase-associated proteins (CAPs) are highly conserved, ubiquitous actin binding proteins that are involved in...
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[NMR paper] Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization
Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization of the FCP1-binding sites of RAP74 and human TFIIB.
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Biochemistry. 2003 Feb 18;42(6):1460-9
Authors: Nguyen BD, Chen HT, Kobor MS, Greenblatt J, Legault P, Omichinski JG
FCP1 (TFIIF-associated CTD phosphatase) is the only known phosphatase specific for the phosphorylated CTD of RNAP II. The phosphatase activity of FCP1 is...
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NMR solution structure of the N-terminal domain of hERG and its interaction with the
NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker.
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Biochem Biophys Res Commun. 2010 Nov 2;
Authors: Li Q, Gayen S, Chen AS, Huang Q, Raida M, Kang C
The human Ether-à-go-go Related Gene (hERG) potassium channel mediates the rapid delayed rectifier current (IKr) in the cardiac action potential. Mutations in the 135 amino acid residue N-terminal domain (NTD) cause channel dysfunction or...
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[NMR paper] The carboxyl-terminal region of human interferon gamma is important for biological ac
The carboxyl-terminal region of human interferon gamma is important for biological activity: mutagenic and NMR analysis.
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Protein Eng. 1991 Feb;4(3):335-41
Authors: Lundell D, Lunn C, Dalgarno D, Fossetta J, Greenberg R, Reim R, Grace M, Narula S
Deletion of nine amino acids from the carboxyl terminus of human IFN gamma (residues 138--146; LFRGRRASQ) resulted in a 7-fold increase in specific antiviral...
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[NMR paper] 1H-NMR investigation of the interaction of the amino terminal domain of the LexA repr
1H-NMR investigation of the interaction of the amino terminal domain of the LexA repressor with a synthetic half-operator.
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J Biomol Struct Dyn. 1991 Dec;9(3):447-61
Authors: Ottleben G, Messori L, Rüterjans H, Kaptein R, Granger-Schnarr M, Schnarr M
A synthetic half-operator DNA-duplex, d(GCTACTGTATGT), containing a portion of the proposed recognition sequence (CTGT) of several "SOS" genes, has been...
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[NMR paper] 1H-NMR investigation of the interaction of the amino terminal domain of the LexA repr
1H-NMR investigation of the interaction of the amino terminal domain of the LexA repressor with a synthetic half-operator.
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J Biomol Struct Dyn. 1991 Dec;9(3):447-61
Authors: Ottleben G, Messori L, Rüterjans H, Kaptein R, Granger-Schnarr M, Schnarr M
A synthetic half-operator DNA-duplex, d(GCTACTGTATGT), containing a portion of the proposed recognition sequence (CTGT) of several "SOS" genes, has been...
NMR characterization of the interaction between the C-terminal domain of interferon-g
Linear Mode
