Design, biological activity and NMR-solution structure of a DNA analogue of yeast tRNAPhe anticodon domain
Design of biologically active DNA analogues of the yeast tRNA Phe anticodon domain, tDNA Phe AC , required the introduction of a d(m 5 C)-dependent, Mg 2+ -induced structural transition and the d(m 1 G) disruption of an intra-loop dC·dG base pair. The modifications were introduced at residues corres...
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Veröffentlicht in: | Nature Structural Biology 1996-01, Vol.3 (1), p.38-44 |
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Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Design of biologically active DNA analogues of the yeast tRNA
Phe
anticodon domain, tDNA
Phe
AC
, required the introduction of a d(m
5
C)-dependent, Mg
2+
-induced structural transition and the d(m
1
G) disruption of an intra-loop dC·dG base pair. The modifications were introduced at residues corresponding to m
5
C-40 and wybutosine-37 in tRNA
Phe
. Modified tDNA
Phe
AC
inhibited translation by 50% at a tDNA
Phe
AC
:ribosome ratio of 8:1. The molecule's structure has been determined by NMR spectroscopy and restrained molecular dynamics with an overall r.m.s.d. of 2.8 Å and 1.7 Å in the stem, and is similar to the tRNA
Phe
anticodon domain in conformation and dimensions. The tDNA
Phe
AC
structure may provide a guide for the design of translation inhibitors as potential therapeutic agents. |
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ISSN: | 1072-8368 1545-9985 |
DOI: | 10.1038/nsb0196-38 |