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Transmembrane Signaling across the Ligand-Gated FhuA Receptor Crystal Structures of Free and Ferrichrome-Bound States Reveal Allosteric Changes
FhuA protein facilitates ligand-gated transport of ferrichrome-bound iron across Escherichia coli outer membranes. X-ray analysis at 2.7 A resolution reveals two distinct conformations in the… Expand
The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand.
The action of 1 alpha, 25-dihydroxyvitamin D3 is mediated by its nuclear receptor (VDR), a ligand-dependent transcription regulator. We report the 1.8 A resolution crystal structure of the complex… Expand
Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α
The crystal structure of the human retinoid-X receptor RXR-α ligand-binding domain reveals a previously undiscovered fold of an antiparallel α-helical sandwich, packed as dimeric units. Two helices… Expand
Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
THE aminoacyl-transfer RNA synthetases (aaRS) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in… Expand
A canonical structure for the ligand-binding domain of nuclear receptors
- J. Wurtz, W. Bourguet, +4 authors H. Gronemeyer
- Biology, Medicine
- Nature Structural Biology
- 1 January 1996
The ability of nuclear receptors (NRs) to activate transcription of target genes requires the binding of cognate ligands to their ligand-binding domains (LBDs). Information provided by the… Expand
Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid
The 2.0-Å crystal structure of the ligand-binding domain (LBD) of the human retinoic acid receptor (RAR)-γ bound to all-trans retinoic acid reveals the ligand-binding interactions and suggests an… Expand
The nuclear receptor ligand-binding domain: structure and function.
In the past few years our understanding of nuclear receptor action has dramatically improved as a result of the elucidation of the crystal structures of the empty (apo) ligand-binding domains of the… Expand
Comparative analysis of ribosomal proteins in complete genomes: an example of reductive evolution at the domain scale.
- O. Lecompte, R. Ripp, J. Thierry, D. Moras, O. Poch
- Medicine, Biology
- Nucleic acids research
- 15 December 2002
A comprehensive investigation of ribosomal genes in complete genomes from 66 different species allows us to address the distribution of r-proteins between and within the three primary domains.… Expand
An operational RNA code for amino acids and possible relationship to genetic code.
- P. Schimmel, R. Giegé, D. Moras, S. Yokoyama
- Biology, Medicine
- Proceedings of the National Academy of Sciences…
- 1 October 1993
RNA helical oligonucleotides that recapitulate the acceptor stems of transfer RNAs, and that are devoid of the anticodon trinucleotides of the genetic code, are aminoacylated by aminoacyl tRNA… Expand
Chemical and biological evolution of a nucleotide-binding protein
Three-dimensional alignment of the common nucleotide binding structure in dehydrogenases, kinases and flavodoxins permits the recognition of homologous amino acids when sequence comparisons alone… Expand