ArticleStructure (London, England : 1993)2004
E. coli trp repressor forms a domain-swapped array in aqueous alcohol.
Article in Structure (London, England : 1993), 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Crystal structures of Val58Ile tryptophan repressor in a domain-swapped array in the presence and absence of L-tryptophan.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Guest-protein incorporation into solvent channels of a protein host crystal (hostal).Acta crystallographica. Section D, Structural biology · 2021Article
- Benefits and constrains of covalency: the role of loop length in protein stability and ligand binding.Scientific reports · 2020Article
- A five-residue motif for the design of domain swapping in proteins.Nature communications · 2019Article
- Mapping the conformational space accessible to catechol-O-methyltransferase.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Environment-dependent long-range structural distortion in a temperature-sensitive point mutant.Protein science : a publication of the Protein Society · 2012Article
- The impact of solubility and electrostatics on fibril formation by the H3 and H4 histones.Protein science : a publication of the Protein Society · 2011Article
- Protein reconstitution and three-dimensional domain swapping: benefits and constraints of covalency.Protein science : a publication of the Protein Society · 2007Review
- RNA-based regulation of genes of tryptophan synthesis and degradation, in bacteria.RNA (New York, N.Y.) · 2007Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The E. coli trp repressor (trpR) homodimer recognizes its palindromic DNA binding site through a pair of flexible helix-turn-helix (HTH) motifs displayed on an intertwined helical core. Flexible N-terminal arms mediate association between dimers bound to tandem DNA sites. The 2.5 A X-ray structure of trpR crystallized in 30% (v/v) isopropanol reveals a substantial conformational rearrangement of HTH motifs and N-terminal arms, with the protein appearing in the unusual form of an ordered 3D domain-swapped supramolecular array. Small angle X-ray scattering measurements show that the self-association properties of trpR in solution are fundamentally altered by isopropanol.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.