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Title: Crystal structures of an HIV-1 integrase aptamer: formation of a water-mediated A•G•G•G•G pentad in an interlocked G-quadruplex
Authors: Ngo, Khac Huy
Liew, Chong Wai
Lattmann, Simon
Winnerdy, Fernaldo Richtia
Phan, Anh Tuân
Keywords: Science::Biological sciences
Issue Date: 2022
Source: Ngo, K. H., Liew, C. W., Lattmann, S., Winnerdy, F. R. & Phan, A. T. (2022). Crystal structures of an HIV-1 integrase aptamer: formation of a water-mediated A•G•G•G•G pentad in an interlocked G-quadruplex. Biochemical and Biophysical Research Communications, 613, 153-158.
Project: NRF-NRFI2017-09 
Journal: Biochemical and Biophysical Research Communications 
Abstract: 93del is a 16-nucleotide G-quadruplex-forming aptamer which can inhibit the activity of the HIV-1 integrase enzyme at nanomolar concentration. Previous structural analyses of 93del using NMR spectroscopy have shown that the aptamer forms an interlocked G-quadruplex structure in K+ solution. Due to its exceptional stability and unique topology, 93del has been used in many different studies involving DNA G-quadruplexes, such as DNA aptamer and multimer design, as well as DNA fluorescence research. To gain further insights on the structure of this unique aptamer, we have determined several high-resolution crystal structures of 93del and its variants. While confirming the overall dimeric interlocked G-quadruplex folding topology previously determined by NMR, our results reveal important detailed structural information, particularly the formation of a water-mediated A•G•G•G•G pentad. These insights allow us to better understand the formation of various structural elements in G-quadruplexes and should be useful for designing and manipulating G-quadruplex scaffolds with desired properties.
ISSN: 0006-291X
DOI: 10.1016/j.bbrc.2022.04.020
Schools: School of Physical and Mathematical Sciences 
Research Centres: NTU Institute of Structural Biology 
Rights: © 2022 Elsevier Inc. All rights reserved. This paper was published in Biochemical and Biophysical Research Communications and is made available with permission of Elsevier Inc.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SPMS Journal Articles

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