Related ArticlesNMR studies of the most conserved RNA domain of the mammalian signal recognition particle (SRP).
RNA. 1996 Dec;2(12):1213-27
Authors: Schmitz U, Freymann DM, James TL, Keenan RJ, Vinayak R, Walter P
Mammalian signal recognition particle (SRP) and its homologues exhibit a phylogenetically conserved RNA domain, whose predicted secondary structure exhibits a hairpin motif with two bulged regions. Two RNA fragments comprising one (24 nt) or two (43 nt) of the conserved bulges were studied. Each fragment binds specifically to the domain of the Escherichia coli homologue of the SRP54 protein, which is involved in signal sequence recognition. The SRP RNA fragments exhibited a pronounced structural stabilization in the presence of Mg2+. Assignments of all base, H1', H2', and most imino proton resonances in the presence of Mg2+ were obtained for the 24mer RNA via NOE spectroscopy and correlated homonuclear NMR methods. 2D NOE patterns permitted a coarse structural description, revealing a relatively compact A-type geometry for the 24mer without any indications of looped-out nucleotides, syn-oriented bases, or base triplets. The GGAA-loop is structurally very similar to that of the GCAA tetraloop [Heus HA, Pardi A, 1991, Science 253:191-194]. Mg2+ seems to stabilize the structure of the conserved bulged region, which involves G:A and C:A mismatch pairs. Deviations from ideal A-type helicity are found for a larger region than the predicted secondary structure implies. Although no explicit assignment effort has been dedicated to the 43mer yet, striking similarity in chemical shift changes upon addition of Mg2+ allowed some structural conclusions. The bulge present in both RNA fragments exhibits a similar, pronounced flexibility in the absence of Mg2+, indicating that the additional bulge in the 43mer does not stabilize the other bulge.
Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy.
Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy.
Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy.
J Biomol NMR. 2011 Jun 12;
Authors: Sastry M, Xu L, Georgiev IS, Bewley CA, Nabel GJ, Kwong PD
NMR spectroscopic characterization of the structure or the dynamics of proteins generally requires the production of samples isotopically enriched in (15)N, (13)C, or (2)H. The bacterial expression systems currently in use to...
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Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy
Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy
Abstract NMR spectroscopic characterization of the structure or the dynamics of proteins generally requires the production of samples isotopically enriched in 15N, 13C, or 2H. The bacterial expression systems currently in use to obtain isotopic enrichment, however, cannot produce a number of eukaryotic proteins, especially those that require post-translational modifications such as N-linked glycosylation for proper folding or activity. Here, we report the use of an...
[NMR paper] Toward an integrated model of protein-DNA recognition as inferred from NMR studies on
Toward an integrated model of protein-DNA recognition as inferred from NMR studies on the Lac repressor system.
Related Articles Toward an integrated model of protein-DNA recognition as inferred from NMR studies on the Lac repressor system.
Chem Rev. 2004 Aug;104(8):3567-86
Authors: Kalodimos CG, Boelens R, Kaptein R
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[NMR paper] NMR studies of U1 snRNA recognition by the N-terminal RNP domain of the human U1A pro
NMR studies of U1 snRNA recognition by the N-terminal RNP domain of the human U1A protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR studies of U1 snRNA recognition by the N-terminal RNP domain of the human U1A protein.
EMBO J. 1994 Aug 15;13(16):3873-81
Authors: Howe PW, Nagai K, Neuhaus D, Varani G
The RNP domain is a very common motif found in hundreds of proteins, including many protein components of the RNA processing machinery. The 70-90...
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[NMR paper] 1H NMR studies of DNA recognition by the glucocorticoid receptor: complex of the DNA
1H NMR studies of DNA recognition by the glucocorticoid receptor: complex of the DNA binding domain with a half-site response element.
Related Articles 1H NMR studies of DNA recognition by the glucocorticoid receptor: complex of the DNA binding domain with a half-site response element.
Biochemistry. 1991 Dec 17;30(50):11620-4
Authors: Remerowski ML, Kellenbach E, Boelens R, van der Marel GA, van Boom JH, Maler BA, Yamamoto KR, Kaptein R
The complex of the rat glucocorticoid receptor (GR) DNA binding domain (DBD) and half-site sequence of the...
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[NMR paper] 1H NMR studies of DNA recognition by the glucocorticoid receptor: complex of the DNA
1H NMR studies of DNA recognition by the glucocorticoid receptor: complex of the DNA binding domain with a half-site response element.
Related Articles 1H NMR studies of DNA recognition by the glucocorticoid receptor: complex of the DNA binding domain with a half-site response element.
Biochemistry. 1991 Dec 17;30(50):11620-4
Authors: Remerowski ML, Kellenbach E, Boelens R, van der Marel GA, van Boom JH, Maler BA, Yamamoto KR, Kaptein R
The complex of the rat glucocorticoid receptor (GR) DNA binding domain (DBD) and half-site sequence of the...
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[NMR paper] Cadmium-113 NMR studies of the DNA binding domain of the mammalian glucocorticoid rec
Cadmium-113 NMR studies of the DNA binding domain of the mammalian glucocorticoid receptor.
Related Articles Cadmium-113 NMR studies of the DNA binding domain of the mammalian glucocorticoid receptor.
Biochemistry. 1990 Oct 2;29(39):9218-25
Authors: Pan T, Freedman LP, Coleman JE
The DNA binding domain of the mammalian glucocorticoid hormone receptor (GR) contains nine highly conserved cysteine residues, a conservation shared by the superfamily of steroid and thyroid hormone receptors. A fragment consisting of GR residues 407-556, containing...
NMR studies of the most conserved RNA domain of the mammalian signal recognition part
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