Protein-DNA conformational changes in the crystal structure of a lambda Cro-operator complex - Wikidata - awgldk - TriplyDB

Protein-DNA conformational changes in the crystal structure of a lambda Cro-operator complex

Protein-DNA conformational changes in the crystal structure of a lambda Cro-operator complex

http://www.wikidata.org/entity/Q27667167

about

Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains Crystal structure of ribosomal protein L4 shows RNA-binding sites for ribosome incorporation and feedback control of the S10 operon Recognition of dual symmetry by the controller protein C.Esp1396I based on the structure of the transcriptional activation complex Base-pair opening and spermine binding--B-DNA features displayed in the crystal structure of a gal operon fragment: implications for protein-DNA recognition The TetR family of transcriptional repressors.Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees Local conformational changes in the DNA interfaces of proteins.Energetics of the protein-DNA-water interaction.Engineering bacterial transcription regulation to create a synthetic in vitro two-hybrid system for protein interaction assays Transcriptional enhancer related DNA sequences: anomalous 1H NMR NOE crosspeaks Orientation of the Lac repressor DNA binding domain in complex with the left lac operator half site characterized by affinity cleaving.DNA recognition code of transcription factors in the helix-turn-helix, probe helix, hormone receptor, and zinc finger families.How Cro and lambda-repressor distinguish between operators: the structural basis underlying a genetic switch.Hydrogen bonding motifs of protein side chains: descriptions of binding of arginine and amide groups A stationary-phase protein of Escherichia coli that affects the mode of association between the trp repressor protein and operator-bearing DNA Members of the IclR family of bacterial transcriptional regulators function as activators and/or repressors.Protein-induced bending and DNA cyclization.Thermodynamics of Cro protein-DNA interactions Structural aspects of protein-DNA recognition.DNA bending induced by Cro protein binding as demonstrated by gel electrophoresis.The V(D)J recombination signal sequence and kappa B binding protein Rc binds DNA as dimers and forms multimeric structures with its DNA ligands Genetic analysis of the Tn21 mer operator-promoter.Probing site-specific interactions in protein-DNA complexes using heteronuclear NMR spectroscopy and molecular modeling: binding of Cro repressor to OR3.Specific DNA binding by c-Myb: evidence for a double helix-turn-helix-related motif.Studying protein-DNA interactions using atomic force microscopy.Specific contacts between residues in the DNA-binding domain of the TyrR protein and bases in the operator of the tyrP gene of Escherichia coli.DNA-methyltransferase SsoII interaction with own promoter region binding site.Cloning of the early promoters of Pseudomonas aeruginosa bacteriophage D3: sequence of the immunity region of D3 The DNA binding domains of the varicella-zoster virus gene 62 and herpes simplex virus type 1 ICP4 transactivator proteins heterodimerize and bind to DNA.Zebrafish pou[c]: a divergent POU family gene ubiquitously expressed during embryogenesis DNA-binding proteins as site-specific nucleases.DNA-binding induces a major structural transition in a type I methyltransferase.Sequence-dependent bending propensity of DNA as revealed by DNase I: parameters for trinucleotides.Protein-protein interactions directing resolvase site-specific recombination: a structure-function analysis.POU proteins bend DNA via the POU-specific domain.Lac repressor with the helix-turn-helix motif of lambda cro binds to lac operator.Solution structure and dynamics of a designed monomeric variant of the lambda Cro repressor.The transcription activation domains of Fos and Jun induce DNA bending through electrostatic interactions.LSF and NTF-1 share a conserved DNA recognition motif yet require different oligomerization states to form a stable protein-DNA complex.Ultrafast differential flexibility of Cro-protein binding domains of two operator DNAs with different sequences.

P2860

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P2860

Protein-DNA conformational changes in the crystal structure of a lambda Cro-operator complex

http://www.wikidata.org/entity/Q27667167

description

1990 nî lūn-bûn

@nan

1990 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1990 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

1990年の論文

@ja

1990年論文

@yue

1990年論文

@zh-hant

1990年論文

@zh-hk

1990年論文

@zh-mo

1990年論文

@zh-tw

1990年论文

@wuu

name

Protein-DNA conformational cha ...... a lambda Cro-operator complex

@ast

Protein-DNA conformational cha ...... a lambda Cro-operator complex

@en

Protein-DNA conformational cha ...... a lambda Cro-operator complex

@nl

type

label

Protein-DNA conformational cha ...... a lambda Cro-operator complex

@ast

Protein-DNA conformational cha ...... a lambda Cro-operator complex

@en

Protein-DNA conformational cha ...... a lambda Cro-operator complex

@nl

prefLabel

Protein-DNA conformational cha ...... a lambda Cro-operator complex

@ast

Protein-DNA conformational cha ...... a lambda Cro-operator complex

@en

Protein-DNA conformational cha ...... a lambda Cro-operator complex

@nl

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P356

PNAS.87.20.8165

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Protein-DNA conformational cha ...... a lambda Cro-operator complex

@en

P2093

B W Matthews

http://www.w3.org/2001/XMLSchema#string

R G Brennan

http://www.w3.org/2001/XMLSchema#string

S L Roderick

http://www.w3.org/2001/XMLSchema#string

Y Takeda

http://www.w3.org/2001/XMLSchema#string

P2860

Recognition of a DNA operator by the repressor of phage 434: a view at high resolution

Crystal structure of trp repressor/operator complex at atomic resolution

Comparison of the structures of cro and lambda repressor proteins from bacteriophage lambda

Analysis of the sequence-specific interactions between Cro repressor and operator DNA by systematic base substitution experiments.

Base sequence-specific interactions of operator DNA fragments with the lambda-cro repressor coupled with changes in their conformations

DNA sequence determinants of lambda repressor binding in vivo.

Phage lambda Cro protein and cI repressor use two different patterns of specific protein-DNA interactions to achieve sequence specificity in vivo.

The helix-turn-helix DNA binding motif.

Structure of catabolite gene activator protein at 2.9 A resolution suggests binding to left-handed B-DNA.

Structure of the cro repressor from bacteriophage lambda and its interaction with DNA.

P304

8165-9

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scholarly article

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10.1073/PNAS.87.20.8165

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P407

P433

20

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P478

87

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1990-10-01T00:00:00Z

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21008719

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P698

2146682

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P921

protein structure

crystal structure

P932

54913

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