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Volumn 9, Issue 1, 1999, Pages 74-87

Adaptive recognition in RNA complexes with peptides and protein modules

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ARGININE; PEPTIDE; PROTEIN; RNA;

EID: 0032864043     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(99)80010-4     Document Type: Article
Times cited : (93)

References (59)
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    • ••] reached similar conclusions regarding the conformation and intermolecular contacts of the bent α-helical peptides and their GNRA-fold-aligned stem-loop RNA targets. The adopted GNRA fold in this complex was achieved by looping out the fourth residue (a guanine) of the pentaloop sequence. The complex was stabilized by the stacking of a tryptophan residue located towards the C terminus of the N peptide with a loop adenine, resulting in the extension of the purine stack within the GNRA fold.
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    • Specific RNA binding proteins constructed from zinc fingers
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    • Crystal structure of an RNA aptamer-protein complex at 2.8 Å resolution
    • This structure of the MS2 coat protein AB dimer bound to an RNA aptamer and an earlier structure of the complex with wildtype RNA [50] establish a critical role in molecular recognition for the orientation and spatial separation of key specificity-determining adenines positioned in the hairpin loop and bulge of the bound RNAs. These structures reinforce the adaptability of RNA folds to mesh with a fixed protein binding architecture.
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    • Crystal structures of a series of RNA aptamers complexed to the same protein target
    • ••] to include additional MS2 coat protein-RNA aptamer complexes. These new RNA aptamers, one of which is missing a key bulged adenine, still bind the MS2 coat protein dimer through adaptive transitions in a manner that is similar to the wildtype RNA complex. The robustness of the MS2 coat protein-RNA stem-loop system and its ready crystallizability suggest that it could serve as a scaffold for linking nucleic acid motifs in need of structural characterization.
    • ••] to include additional MS2 coat protein-RNA aptamer complexes. These new RNA aptamers, one of which is missing a key bulged adenine, still bind the MS2 coat protein dimer through adaptive transitions in a manner that is similar to the wildtype RNA complex. The robustness of the MS2 coat protein-RNA stem-loop system and its ready crystallizability suggest that it could serve as a scaffold for linking nucleic acid motifs in need of structural characterization.
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