Related ArticlesNMR solution structure of AlcR (1-60) provides insight in the unusual DNA binding properties of this zinc binuclear cluster protein.
J Mol Biol. 2000 Jan 28;295(4):729-36
Authors: Cerdan R, Cahuzac B, Félenbok B, Guittet E
The three-dimensional structure of the DNA-binding domain (residues 1-60) of the ethanol regulon transcription factor AlcR from Aspergillus nidulans has been solved by NMR. This domain belongs to the zinc binuclear cluster class. Although the core of the protein is similar to previously characterized structures, consisting of two helices organized around a Zn(2)Cys(6 )motif, the present structure presents important variations, among them the presence of two supplementary helices. This structure gives new insight into the understanding of the AlcR specificities in DNA binding such as longer consensus half-sites, in vitro monomeric binding but in vivo multiple repeat transcriptional activation, either in direct or inverse orientations. The presence of additional contacts of the protein with its DNA target can be predicted from a model proposed for the interaction with the consensus DNA target. The clustering of accessible negative charges on helix 2 delineates a possible interaction site for other determinants of the transcriptional machinery, responsible for the fine tuning of the selection of the AlcR cognate sites.
Chemical Shifts for the Unusual DNA Structure in Pf1 Bacteriophage from Dynamic-Nuclear-Polarization-Enhanced Solid-State NMR Spectroscopy.
Chemical Shifts for the Unusual DNA Structure in Pf1 Bacteriophage from Dynamic-Nuclear-Polarization-Enhanced Solid-State NMR Spectroscopy.
Chemical Shifts for the Unusual DNA Structure in Pf1 Bacteriophage from Dynamic-Nuclear-Polarization-Enhanced Solid-State NMR Spectroscopy.
J Am Chem Soc. 2011 Aug 22;
Authors: Sergeyev IV, Day LA, Goldbourt A, McDermott AE
Abstract
Solid state NMR spectra, including dynamic nuclear polarization enhanced 400 MHz spectra acquired at 100K, as well as non-DNP spectra at a variety of field strengths and...
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[NMR paper] The solution NMR structure of Antheraea polyphemus PBP provides new insight into pher
The solution NMR structure of Antheraea polyphemus PBP provides new insight into pheromone recognition by pheromone-binding proteins.
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J Mol Biol. 2004 Mar 19;337(2):443-51
Authors: Mohanty S, Zubkov S, Gronenborn AM
Pheromone-binding proteins (PBPs) located in the antennae of male moth species play an important role in olfaction. They are carrier proteins, believed to transport volatile...
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[NMR paper] NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein
NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein that is selectively cytotoxic to cancer cells.
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Biochemistry. 2004 Feb 24;43(7):1854-61
Authors: Rosal R, Pincus MR, Brandt-Rauf PW, Fine RL, Michl J, Wang H
We have recently found that a peptide from the mdm-2 binding domain of the p53 protein induced rapid membranolytic necrosis of a variety of different human...
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[NMR paper] Solution structure of the two N-terminal RNA-binding domains of nucleolin and NMR stu
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J Mol Biol. 2000 Oct 20;303(2):227-41
Authors: Allain FH, Gilbert DE, Bouvet P, Feigon J
Nucleolin is an abundant 70 kDa nucleolar protein involved in many aspects of ribosomal RNA biogenesis. The central region of nucleolin contains four tandem consensus RNA-binding domains...
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[NMR paper] NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+
NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump.
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Biochemistry. 1999 Sep 21;38(38):12320-32
Authors: Elshorst B, Hennig M, Försterling H, Diener A, Maurer M, Schulte P, Schwalbe H, Griesinger C, Krebs J, Schmid H, Vorherr T, Carafoli E
The three-dimensional structure of the complex between calmodulin (CaM) and a peptide corresponding to the N-terminal portion of the CaM-binding domain of the...
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[NMR paper] Unusual helix-containing greek keys in development-specific Ca(2+)-binding protein S.
Unusual helix-containing greek keys in development-specific Ca(2+)-binding protein S. 1H, 15N, and 13C assignments and secondary structure determined with the use of multidimensional double and triple resonance heteronuclear NMR spectroscopy.
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Biochemistry. 1994 Mar 8;33(9):2409-21
Authors: Bagby S,...
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[NMR paper] Unusual helix-containing greek keys in development-specific Ca(2+)-binding protein S.
Unusual helix-containing greek keys in development-specific Ca(2+)-binding protein S. 1H, 15N, and 13C assignments and secondary structure determined with the use of multidimensional double and triple resonance heteronuclear NMR spectroscopy.
Related Articles Unusual helix-containing greek keys in development-specific Ca(2+)-binding protein S. 1H, 15N, and 13C assignments and secondary structure determined with the use of multidimensional double and triple resonance heteronuclear NMR spectroscopy.
Biochemistry. 1994 Mar 8;33(9):2409-21
Authors: Bagby S,...
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[NMR paper] NMR analysis of the residual structure in the denatured state of an unusual mutant of
NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease.
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Structure. 1993 Oct 15;1(2):121-34
Authors: Shortle D, Abeygunawardana C
BACKGROUND: Staphylococcal nuclease is a well-developed model system for analyzing the effects of mutations on protein folding and stability. Substitution of glycine 88 with valine (Gly88Val) destabilizes staphylococcal nuclease by 1.0...
NMR solution structure of AlcR (1-60) provides insight in the unusual DNA binding pro
Linear Mode
