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- W47397845 abstract "Publisher Summary A number of protein-RNA interactions in the ribosome have been conserved during evolution and it is the most ancient examples of protein-nucleic acid recognition in the cell. Lll recognizes a 58 nucleotide ribosomal RNA (rRNA) fragment. The structure of a 76 residue Lll RNA-binding domain, both free in solution and bound to its RNA target, has been solved by magnetic resonance (NMR) methods, and the RNA-binding surface defined by site directed mutagenesis and nuclear NMR. Two main features contribute to recognition: an α-helix and a large, flexible loop that adopts a specific conformation upon binding. The protein structure is remarkably similar to that of the homeodomain class of Deoxyribonucleic acid (DNA)-binding proteins. Phylogenetic analysis has been very helpful in suggesting key components of the RNA tertiary structure and the Lll recognition surface, the most highly conserved residues (either protein or RNA) tend to be required either for folding or for recognition. However, the phylogenetic record also suggests that bacterial, archaeal and eukaryotic complexes use slightly different strategies for recognition." @default.
- W47397845 created "2016-06-24" @default.
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- W47397845 date "1998-01-01" @default.
- W47397845 modified "2023-09-26" @default.
- W47397845 title "Protein-RNA Recognition in a Highly Conserved Ribosomal Domain Targeted by Thiazole Antibiotics" @default.
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- W47397845 doi "https://doi.org/10.1016/b978-012233210-4/50009-8" @default.
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