229D

DNA ANALOG OF YEAST TRANSFER RNA PHE ANTICODON DOMAIN WITH MODIFIED BASES 5-METHYL CYTOSINE AND 1-METHYL GUANINE

Summary for 229D

• Entry DOI: 10.2210/pdb229d/pdb
• Descriptor: DNA (5'-D(*CP*CP*AP*GP*AP*CP*(UMP)P*GP*AP*AP*(MG1)P*AP*(UMP)P*(5CM)P*(UMP)P*GP*G)-3') (1 entity in total)
• Functional Keywords: dna, transfer rna, anticodon, hairpin loop
• Total number of polymer chains: 1
• Total formula weight: 5222.39

Authors

Basti, M.M.,Stuart, J.W.,Lam, A.T.,Guenther, R.,Agris, P.F. (deposition date: 1995-08-16, release date: 1995-12-07, Last modification date: 2024-05-22)

Primary citation

Basti, M.M.,Stuart, J.W.,Lam, A.T.,Guenther, R.,Agris, P.F.
Design, biological activity and NMR-solution structure of a DNA analogue of yeast tRNA(Phe) anticodon domain.
Nat.Struct.Biol., 3:38-44, 1996

PubMed 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.

PubMed: 8548453
DOI: 10.1038/nsb0196-38

Experimental method

SOLUTION NMR