Preferred binding sites for [N-MeCys(3),N-MeCys(7)]TANDEM determined using a universal footprinting substrate
Preferred binding sites for [N-MeCys(3),N-MeCys(7)]TANDEM determined using a universal footprinting substrate
We have prepared a novel footprinting substrate which contains all 136 tetranucleotide sequences and have used this to determine the preferred binding sites for the synthetic quinoxaline antibiotic [N-MeCys3,N-MeCys7]TANDEM. We find that, although the ligand binds to all TpA steps, it binds best to the tetranucleotide sequence ATAT and shows only weak interaction with TTAA and GTAC. The best binding sites contain the sequences ATAX and XTAT.
footprinting, TANDEM, DNase I, quinoxaline antibiotic
246-250
Lavesa, M.
f3720d36-5310-4826-830e-28173e520472
Fox, K.R.
9da5debc-4e45-473e-ab8c-550d1104659f
1 June 2001
Lavesa, M.
f3720d36-5310-4826-830e-28173e520472
Fox, K.R.
9da5debc-4e45-473e-ab8c-550d1104659f
Lavesa, M. and Fox, K.R.
(2001)
Preferred binding sites for [N-MeCys(3),N-MeCys(7)]TANDEM determined using a universal footprinting substrate.
Analytical Biochemistry, 293 (2), .
(doi:10.1006/abio.2001.5124).
Abstract
We have prepared a novel footprinting substrate which contains all 136 tetranucleotide sequences and have used this to determine the preferred binding sites for the synthetic quinoxaline antibiotic [N-MeCys3,N-MeCys7]TANDEM. We find that, although the ligand binds to all TpA steps, it binds best to the tetranucleotide sequence ATAT and shows only weak interaction with TTAA and GTAC. The best binding sites contain the sequences ATAX and XTAT.
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Submitted date: 17 January 2001
Published date: 1 June 2001
Keywords:
footprinting, TANDEM, DNase I, quinoxaline antibiotic
Identifiers
Local EPrints ID: 55960
URI: http://eprints.soton.ac.uk/id/eprint/55960
ISSN: 0003-2697
PURE UUID: e1a60144-1814-4a92-ad30-2f38f0fd00f7
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Date deposited: 06 Aug 2008
Last modified: 16 Mar 2024 02:36
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Author:
M. Lavesa
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