Related ArticlesPrion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy.
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, although there are indications of a role in signal transduction in neurons. To gain further insight into the functional properties of cellular PrP, this paper investigated the binding of the C-terminal SH3 domain of the murine growth factor receptor-bound protein 2 (Grb2) to the murine PrP, using NMR, fluorescence, and circular dichroism spectroscopy. The SH3-binding site in murine PrP was thus found to be in the highly conserved region of residues 100-109, which contains prolines in positions 101 and 104. The protein-protein interaction, with a K(D) value of 5.5 microM, is abolished when either of these two prolines is replaced by leucine. In humans, two corresponding Pro --> Leu exchanges are found in patients who present with the Gerstmann-Sträussler-Scheinker syndrome. The results of the present study thus indicate a possible mechanism by which amino acid exchanges could influence a specific protein-protein interaction in a complex signal transduction cascade, which might be of functional significance in health and disease.
Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion
Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion
Abstract We present the de novo resonance assignments for the crystalline 33 kDa C-terminal domain of the Ure2 prion using an optimized set of five 3D solid-state NMR spectra. We obtained, using a single uniformly 13C, 15N labeled protein sample, sequential chemical-shift information for 74% of the N, Cα, Cβ triples, and for 80% of further side-chain resonances for these spin systems. We describe the procedures and protocols devised, and discuss possibilities and limitations of the...
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Extensive de novo solid-state NMR assignments of the 33*kDa C-terminal domain of the Ure2 prion.
Extensive de novo solid-state NMR assignments of the 33*kDa C-terminal domain of the Ure2 prion.
Extensive de novo solid-state NMR assignments of the 33*kDa C-terminal domain of the Ure2 prion.
J Biomol NMR. 2011 Jul 31;
Authors: Habenstein B, Wasmer C, Bousset L, Sourigues Y, Schütz A, Loquet A, Meier BH, Melki R, Böckmann A
We present the de novo resonance assignments for the crystalline 33*kDa C-terminal domain of the Ure2 prion using an optimized set of five 3D solid-state NMR spectra. We obtained, using a single uniformly (13)C, (15)N labeled...
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08-02-2011 11:40 AM
[NMR paper] NMR characterization of the interaction between the C-terminal domain of interferon-g
NMR characterization of the interaction between the C-terminal domain of interferon-gamma and heparin-derived oligosaccharides.
Related Articles NMR characterization of the interaction between the C-terminal domain of interferon-gamma and heparin-derived oligosaccharides.
Biochem J. 2004 Nov 15;384(Pt 1):93-9
Authors: Vanhaverbeke C, Simorre JP, Sadir R, Gans P, Lortat-Jacob H
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...
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11-24-2010 10:03 PM
[NMR paper] NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with
NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers.
Related Articles NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers.
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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11-24-2010 09:51 PM
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.
NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker.
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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11-09-2010 11:29 AM
[NMR paper] Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronu
Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three- and four-dimensional NMR spectroscopy.
Related Articles Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three- and four-dimensional NMR spectroscopy.
Biochemistry. 1995 Dec 26;34(51):16596-607
Authors: Hardman CH, Broadhurst RW, Raine AR, Grasser KD, Thomas JO, Laue ED
HMG1 has two homologous, folded DNA-binding domains ("HMG boxes"), A and B, linked by a short basic region to an acidic C-terminal domain....
[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.
Related Articles 1H-NMR investigation of the interaction of the amino terminal domain of the LexA repressor with a synthetic half-operator.
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...