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The ligand-binding domain of nuclear receptors appears to contain a common fold that generates a conserved ligand-binding pocket. Their transcriptional activity is induced by ligand through realignment of a Gterminal helix to form a novel interacting surface.
Neutron diffraction studies show that the inositol ring in the headgroup of phosphatidylinositol extends perpendicular to the membrane surface but that phosphorylation of the 4-position causes the ring to tilt over.
The stuctures of the co-chaperonin GroES and of the GroEL•ATPγS complex raise a host of tantalizing questions and whet the appetite for even more challenging structures, the various GroEL•nucleotide•GroES complexes which facilitate folding.
The three-dimensional structure of the N-terminal domain of an archaeal TFIIB, which has high sequence homology with eucaryal analogues, is strikingly similar to that of the C-terminal zinc ribbon of the eucaryal transcription elongation factor TFIIS.
Extensive three-dimensional structural resemblances between biotin carboxylase and the ADP-forming peptide synthetases, represented by glutathione synthetase and D-Ala:D-Ala ligase, reveal a previously unsuspected evolutionary relationship between two major families of ADP-forming ligases.
The crystal structure of a 92,000 Mr fragment of yeast DNA topoisomerase II suggests how the enzyme can facilitate the passage of one segment of duplex DNA through a double-stranded break in another.