229d
From Proteopedia
DNA ANALOG OF YEAST TRANSFER RNA PHE ANTICODON DOMAIN WITH MODIFIED BASES 5-METHYL CYTOSINE AND 1-METHYL GUANINE
Overview
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.
About this Structure
Full crystallographic information is available from OCA.
Reference
Design, biological activity and NMR-solution structure of a DNA analogue of yeast tRNA(Phe) anticodon domain., Basti MM, Stuart JW, Lam AT, Guenther R, Agris PF, Nat Struct Biol. 1996 Jan;3(1):38-44. PMID:8548453 Page seeded by OCA on Sat May 3 18:20:38 2008
Categories: Agris, P F. | Basti, M M. | Guenther, R. | Lam, A T. | Stuart, J W. | Anticodon | Dna | Hairpin loop | Transfer rna
