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Design, biological activity and NMR-solution structure of a DNA analogue of yeast tRNAPhe anticodon domain
- Source :
- Nature Structural Biology. 3:38-44
- Publication Year :
- 1996
- Publisher :
- Springer Science and Business Media LLC, 1996.
-
Abstract
- Design of biologically active DNA analogues of the yeast tRNA(Phe) anticodon domain, tDNAPheAC, required the introduction of a d(m5C)-dependent, Mg(2+)-induced structural transition and the d(m1G) disruption of an intra-loop dC.dG base pair. The modifications were introduced at residues corresponding to m5C-40 and wybutosine-37 in tRNA(Phe). Modified tDNAPheAC inhibited translation by 50% at a tDNAPheAC: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 A and 1.7 A in the stem, and is similar to the tRNA(Phe) anticodon domain in conformation and dimensions. The tDNAPheAC structure may provide a guide for the design of translation inhibitors as potential therapeutic agents.
- Subjects :
- Magnetic Resonance Spectroscopy
Base Sequence
Molecular Structure
Stereochemistry
Base pair
Molecular Sequence Data
Fungal genetics
RNA, Fungal
Translation (biology)
Saccharomyces cerevisiae
Nuclear magnetic resonance spectroscopy
Biology
Biochemistry
Ribosome
RNA, Transfer, Phe
chemistry.chemical_compound
chemistry
Structural Biology
Transfer RNA
Anticodon
Genetics
A-DNA
DNA, Fungal
DNA
Subjects
Details
- ISSN :
- 10728368
- Volume :
- 3
- Database :
- OpenAIRE
- Journal :
- Nature Structural Biology
- Accession number :
- edsair.doi.dedup.....4304f6b5f1939ed2f476aa56424df898