Related ArticlesNMR analysis of CYP1(HAP1) DNA binding domain-CYC1 upstream activation sequence interactions: recognition of a CGG trinucleotide and of an additional thymine 5 bp downstream by the zinc cluster and the N-terminal extremity of the protein.
Nucleic Acids Res. 1997 Aug 1;25(15):3042-50
Authors: Vuidepot AL, Bontems F, Gervais M, Guiard B, Shechter E, Lallemand JY
The DNA binding domain of the yeast transcriptional activator CYP1(HAP1) contains a zinc-cluster structure. The structures of the DNA binding domain-DNA complexes of two other zinc-cluster proteins (GAL4 and PPR1) have been studied by X-ray crystallography. Their binding domains present, besides the zinc cluster, a short linker peptide and a dimerization element. They recognize, as homodimers, two rotationally symmetric CGG trinucleotides, the linker peptide and the dimerization element playing a crucial role in binding specificity. Surprisingly, CYP1 recognizes degenerate forms of a direct repeat, CGGnnnTAnCGGnnnTA, and the role of its linker is under discussion. To better understand the binding specificity of CYP1, we have studied, by NMR, the interaction between the CYP1(55-126) peptide and two DNA fragments derived from the CYC1 upstream activation sequence 1B. Our data indicate that CYP1(55-126) interacts with a CGG and with a thymine 5 bp downstream. The CGG trinucleotide is recognized by the zinc cluster in the major groove, as for GAL4 and PPR1, and the thymine is bound in the minor groove by the N-terminal region, which possesses a basic stretch of arginyl and lysyl residues. This suggests that the CYP1(55-126) N-terminal region could play a role in the affinity and/or specificity of the interaction with its DNA targets, in contrast to GAL4 and PPR1.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Biochimie. 2011 Sep 22;
Authors: Galea CA, Mobli M, McNeil KA, Mulhern TD, Wallace JC, King GF, Forbes BE, Norton RS
Abstract
The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to 6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In addition...
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09-30-2011 06:00 AM
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Biochimie. 2011 Sep 22;
Authors: Galea CA, Mobli M, McNeil KA, Mulhern TD, Wallace JC, King GF, Forbes BE, Norton RS
Abstract
The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to 6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In...
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09-30-2011 05:59 AM
NMR Analysis of a Kinetically Trapped Intermediate of a Disulfide-Deficient Mutant of the Starch-Binding Domain of Glucoamylase.
NMR Analysis of a Kinetically Trapped Intermediate of a Disulfide-Deficient Mutant of the Starch-Binding Domain of Glucoamylase.
NMR Analysis of a Kinetically Trapped Intermediate of a Disulfide-Deficient Mutant of the Starch-Binding Domain of Glucoamylase.
J Mol Biol. 2011 Jul 23;
Authors: Sugimoto H, Noda Y, Segawa SI
A thermally unfolded disulfide-deficient mutant of the starch-binding domain of glucoamylase refolds into a kinetically trapped metastable intermediate when subjected to a rapid lowering of temperature. We attempted to characterise...
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08-02-2011 11:40 AM
NMR analysis reveals 17?-estradiol induced conformational change in ER? ligand binding domain expressed in E. coli.
NMR analysis reveals 17?-estradiol induced conformational change in ER? ligand binding domain expressed in E. coli.
NMR analysis reveals 17?-estradiol induced conformational change in ER? ligand binding domain expressed in E. coli.
Mol Biol Rep. 2010 Dec 12;
Authors: Paramanik V, Thakur MK
Nuclear magnetic resonance (NMR) spectroscopy is a useful biophysical technique to study the ligand-protein interaction. In this report, we have used bacterially produced ER? and its domains for studying the functional analysis of ligand-protein interaction....
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[NMR paper] NMR and ICP spectroscopic analysis of the DNA-binding domain of the Drosophila GCM pr
NMR and ICP spectroscopic analysis of the DNA-binding domain of the Drosophila GCM protein reveals a novel Zn2+ -binding motif.
Related Articles NMR and ICP spectroscopic analysis of the DNA-binding domain of the Drosophila GCM protein reveals a novel Zn2+ -binding motif.
Protein Eng. 2003 Apr;16(4):247-54
Authors: Shimizu M, Hiroaki H, Kohda D, Hosoya T, Akiyama-Oda Y, Hotta Y, Morita EH, Morikawa K
Drosophila GCM (glial cell missing) is a novel DNA-binding protein that determines the fate of glial precursors from the neural default to glia....
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[NMR paper] NMR analysis of intra- and inter-molecular stems in the dimerization initiation site
NMR analysis of intra- and inter-molecular stems in the dimerization initiation site of the HIV-1 genome.
Related Articles NMR analysis of intra- and inter-molecular stems in the dimerization initiation site of the HIV-1 genome.
J Biochem. 2000 Apr;127(4):681-6
Authors: Takahashi K, Baba S, Hayashi Y, Koyanagi Y, Yamamoto N, Takaku H, Kawai G
Two positive-strand HIV-1 genomic RNAs form a dimer in virion particles through interaction of the dimerization initiation sites (DIS). The DIS RNA fragment spontaneously formed a "loose-dimer" and was...
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[NMR paper] Inter-tryptophan distances in rat cellular retinol binding protein II by solid-state
Inter-tryptophan distances in rat cellular retinol binding protein II by solid-state NMR.
Related Articles Inter-tryptophan distances in rat cellular retinol binding protein II by solid-state NMR.
Biochemistry. 1993 May 4;32(17):4560-3
Authors: McDowell LM, Holl SM, Qian SJ, Li E, Schaefer J
Structural constraints for the tryptophans in rat cellular retinol binding protein II (CRBP II) have been obtained by rotational-echo double-resonance (REDOR) solid-state NMR. CRBP II was labeled with L-tryptophan and L-tryptophan. The 13C-19F dipolar...
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[NMR paper] The NMR structure of the activation domain isolated from porcine procarboxypeptidase
The NMR structure of the activation domain isolated from porcine procarboxypeptidase B.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles The NMR structure of the activation domain isolated from porcine procarboxypeptidase B.
EMBO J. 1991 Jan;10(1):11-5
Authors: Vendrell J, Billeter M, Wider G, Avilés FX, Wüthrich K
The three-dimensional structure of the activation domain isolated from porcine pancreatic procarboxypeptidase B was determined using 1H NMR...
NMR analysis of CYP1(HAP1) DNA binding domain-CYC1 upstream activation sequence inter
Linear Mode
