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Title: Characterisation of an aptamer against the Runt domain of AML1 (RUNX1) by NMR and mutational analyses
Authors: Takada, Kenta
Amano, Ryo
Nomura, Yusuke
Tanaka, Yoichiro
Sugiyama, Shigeru
Nagata, Takashi  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0002-3733-2709 (unconfirmed)
Katahira, Masato  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0003-0336-7660 (unconfirmed)
Nakamura, Yoshikazu
Kozu, Tomoko
Sakamoto, Traiichi
Author's alias: 永田, 祟
片平, 正人
Keywords: AML1
aptamer
Mutation
NMR
Issue Date: Feb-2018
Publisher: Wiley-Blackwell
Journal title: FEBS Open Bio
Volume: 8
Issue: 2
Start page: 264
End page: 270
Abstract: Since the invention of systematic evolution of ligands by exponential enrichment, many short oligonucleotides (or aptamers) have been reported that can bind to a wide range of target molecules with high affinity and specificity. Previously, we reported an RNA aptamer that shows high affinity to the Runt domain (RD) of the AML1 protein, a transcription factor with roles in haematopoiesis and immune function. From kinetic and thermodynamic studies, it was suggested that the aptamer recognises a large surface area of the RD, using numerous weak interactions. In this study, we identified the secondary structure by nuclear magnetic resonance spectroscopy and performed a mutational study to reveal the residue critical for binding to the RD. It was suggested that the large contact area was formed by a DNA‐mimicking motif and a multibranched loop, which confers the high affinity and specificity of binding.
Rights: © 2017 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
URI: http://hdl.handle.net/2433/230576
DOI(Published Version): 10.1002/2211-5463.12368
PubMed ID: 29435416
Appears in Collections:Journal Articles

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