This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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
229D is a Protein complex structure of sequences from [1]. 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 Thu Feb 21 16:21:18 2008
Categories: Protein complex | Agris, P F. | Basti, M M. | Guenther, R. | Lam, A T. | Stuart, J W. | Anticodon | Dna | Hairpin loop | Transfer rna
