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Structure of tandem and its implication for bifunctional intercalation into dna

Viswamitra, MA and Egert, E and Sheldrick, GM and Jones, PG and Waring, MJ and Wakelin, LP and Olsen, RK and Cruse, WB and Kennard, O (1981) Structure of tandem and its implication for bifunctional intercalation into dna. In: Nature, 289 (5800). pp. 817-819.

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Official URL: http://www.nature.com/nature/journal/v289/n5800/ab...

Abstract

Quinoxaline antibiotics (Fig. 1a, b) form a useful group of compounds for the study of drug–nucleic acid interactions1,2. They consist of a cross-bridged cyclic octadepsipeptide, variously modified, bearing two quinoxaline chromophores. These antibiotics intercalate bifunctionally into DNA2,3 probably via the narrow groove, forming a complex in which, most probably, two base pairs are sandwiched between the chromophores4,5. Depending on the nature of their sulphur-containing cross-bridge and modifications to their amino acid side chains, they display characteristic patterns of nucleotide sequence selectivity when binding to DNAs of different base composition and to synthetic polydeoxynucleotides4,6,7. This specificity has been tentatively ascribed to specific hydrogen-bonding interactions between functional groups in the DNA and complementary moieties on the peptide ring2,4,5. Variations in selectivity have been attributed both to changes in the conformation of the peptide backbone6 and no modifications of the cross-bridge7. These suggestions were made, however, in the absence of firm knowledge about the three-dimensional structure and conformation of the antibiotic molecules. We now report the X-ray structure analysis of the synthetic analogue of the antibiotic triostin A, TANDEM (des-N-tetramethyl triostin A) (Fig. 1c), which binds preferentially to alternating adenine-thymine sequences7. The X-ray structure provides a starting point for exploring the origin of this specificity and suggests possible models for the binding of other members of the quinoxaline series.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Nature Publishing Group.
Department/Centre: Others
Date Deposited: 17 Feb 2012 05:44
Last Modified: 17 Feb 2012 05:44
URI: http://eprints.iisc.ernet.in/id/eprint/43286

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