The crystal structure of trp aporepressor at 1.8 A shows how binding tryptophan enhances DNA affinity.
about
The tryptophan repressor sequence is highly conserved among the EnterobacteriaceaeCorepressor-induced organization and assembly of the biotin repressor: A model for allosteric activation of a transcriptional regulatorA protein functional leap: how a single mutation reverses the function of the transcription regulator TetRCrystal structure of the P2 C-repressor: a binder of non-palindromic direct DNA repeatsThe Agrobacterium tumefaciens Transcription Factor BlcR Is Regulated via OligomerizationEnvironment-dependent long-range structural distortion in a temperature-sensitive point mutantThe X-ray structure of the PurR-guanine-purF operator complex reveals the contributions of complementary electrostatic surfaces and a water-mediated hydrogen bond to corepressor specificity and binding affinityEffect of mutation at the interface of Trp-repressor dimeric protein: a steered molecular dynamics simulation.The solution structures of Escherichia coli trp repressor and trp aporepressor at an intermediate resolution.A negative electrostatic determinant mediates the association between the Escherichia coli trp repressor and its operator DNA.Structural homology between rbs repressor and ribose binding protein implies functional similarity.NMR observation of individual molecules of hydration water bound to DNA duplexes: direct evidence for a spine of hydration water present in aqueous solution.The folding energy landscape of the dimerization domain of Escherichia coli Trp repressor: a joint experimental and theoretical investigation.Nanosensor detection of an immunoregulatory tryptophan influx/kynurenine efflux cycle.Gel retardation at low pH resolves trp repressor-DNA complexes for quantitative study.Studies of the Escherichia coli Trp repressor binding to its five operators and to variant operator sequences.The DNA target of the trp repressorSecond-site revertants of Escherichia coli trp repressor mutants.Mutant tryptophan aporepressors with altered specificities of corepressor recognition.Transition metal ion activation of DNA binding by the diphtheria tox repressor requires the formation of stable homodimers.Electrostatic forces contribute to interactions between trp repressor dimers.Formation of repressor-inducer-operator ternary complex: negative cooperativity of d-camphor binding to CamR.Modulation of the stability of a gene-regulatory protein dimer by DNA and cAMP.Preliminary crystallography confirms that the archaeal DNA-binding and tryptophan-sensing regulator TrpY is a dimer.NMR studies of the Escherichia coli Trp repressor.trpRs operator complex.Molecular mechanism of tryptophan-dependent transcriptional regulation in Chlamydia trachomatis.Operator recognition by the ROK transcription factor family members, NagC and MlcThe NH2-terminal arms of trp repressor participate in repressor/operator association.NikR-operator complex structure and the mechanism of repressor activation by metal ions.Genomic analysis of the hierarchical structure of regulatory networksE. coli trp repressor forms a domain-swapped array in aqueous alcohol.The DnrN protein of Streptomyces peucetius, a pseudo-response regulator, is a DNA-binding protein involved in the regulation of daunorubicin biosynthesis.Luminescence of ruthenium(II) polypyridyls: evidence for intercalative binding to Z-DNA.NADP, corepressor for the Bacillus catabolite control protein CcpA.Molecular dynamics studies of a DNA-binding protein: 2. An evaluation of implicit and explicit solvent models for the molecular dynamics simulation of the Escherichia coli trp repressor.Tryptophan replacements in the trp aporepressor from Escherichia coli: probing the equilibrium and kinetic folding modelsResolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants.A structural role for arginine in proteins: multiple hydrogen bonds to backbone carbonyl oxygens.Deciphering the transcriptional regulatory logic of amino acid metabolism.The Tumbleweed: towards a synthetic proteinmotor.
P2860
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P2860
The crystal structure of trp aporepressor at 1.8 A shows how binding tryptophan enhances DNA affinity.
description
1987 nî lūn-bûn
@nan
1987 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
The crystal structure of trp a ...... ptophan enhances DNA affinity.
@ast
The crystal structure of trp a ...... ptophan enhances DNA affinity.
@en
The crystal structure of trp a ...... ptophan enhances DNA affinity.
@nl
type
label
The crystal structure of trp a ...... ptophan enhances DNA affinity.
@ast
The crystal structure of trp a ...... ptophan enhances DNA affinity.
@en
The crystal structure of trp a ...... ptophan enhances DNA affinity.
@nl
prefLabel
The crystal structure of trp a ...... ptophan enhances DNA affinity.
@ast
The crystal structure of trp a ...... ptophan enhances DNA affinity.
@en
The crystal structure of trp a ...... ptophan enhances DNA affinity.
@nl
P2093
P356
P1433
P1476
The crystal structure of trp a ...... ptophan enhances DNA affinity.
@en
P2093
Joachimiak A
Otwinowski Z
Schevitz RW
P2888
P304
P356
10.1038/327591A0
P407
P577
1987-06-01T00:00:00Z
P5875
P6179
1004279603