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The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand.
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Transmembrane Signaling across the Ligand-Gated FhuA Receptor Crystal Structures of Free and Ferrichrome-Bound States Reveal Allosteric Changes
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A canonical structure for the ligand-binding domain of nuclear receptors
TLDR
Mutant studies support a general mechanism for ligand-induced activation deduced from the comparison of the transcriptionally active RARγ holo- and inactive RXRα apo-LBD structures.
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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…
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Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
TLDR
Surprisingly, this partition of aaRS in two classes is found to be strongly correlated on the functional level with the acylation occurring either on the 2′ OH or 3′ OH of the ribose of the last nucleotide of tRNA.
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The nuclear receptor ligand-binding domain: structure and function.
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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…
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Comparative analysis of ribosomal proteins in complete genomes: an example of reductive evolution at the domain scale.
TLDR
This first documented case of reductive evolution at the domain scale provides a new framework for discussing the shape of the universal tree of life and the selective forces directing the evolution of prokaryotes.
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An operational RNA code for amino acids and possible relationship to genetic code.
TLDR
Members of the two different classes of tRNA synthetases are, like tRNAs, organized into two major domains, and the emergence of the genetic from the operational RNA code could occur when the second domain of synthetase was added with the anticodon-containing domain of t RNAs.
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An attempt to unify the structure of polymerases.
TLDR
A DNA polymerase sequence from bacteriophage SPO2 was found to be homologous to the polymerase domain of the Klenow fragment of polymerase I from Escherichia coli, which is known to be closely related to those from Staphylococcus pneumoniae, Thermus aquaticus and bacteriophile T7 and T5.
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