Structural analysis of peptide identified from the 2KRR domain of the nucleolin protein with a c-Myc G4 structure using biophysical and biochemical methods-Reference-Cited by-同舟云学术

Structural analysis of peptide identified from the 2KRR domain of the nucleolin protein with a c-Myc G4 structure using biophysical and biochemical methods

Published:2024 Issue:32 Volume:14 Page:22801-22808
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Kaur Sarvpreet¹,Kundu Nikita¹,Sharma Taniya¹,Shankaraswamy J.²,Singh Sweta³^ORCID,Saxena Sarika¹^ORCID

Affiliation:

1. Amity Institute of Biotechnology, Amity University Uttar Pradesh, Noida 201313, India

2. Department of Fruit Science, College of Horticulture, Mojerla, Sri Konda Laxman Telangana State Horticultural University, 509382, Telangana, India

3. Institute of Nuclear Medicine and Allied Sciences (INMAS), DRDO, Brig. S. K. Mazumdar Marg, Delhi-110054, India

Abstract

The stabilization of c-Myc G4 structure is reported by binding of the peptide (derived from the 2KRR domain of the nucleolin protein called the Nu peptide) in the loop region of the G-quadruplex structure by stacking interactions.

Funder

Department of Biotechnology, Ministry of Science and Technology, India

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/RA/D4RA02785J

Reference20 articles.

1. Formation of parallel four-stranded complexes by guanine-rich motifs in DNA and its implications for meiosis

2. Quadruplex DNA: sequence, topology and structure

3. Prevalence of quadruplexes in the human genome

4. Direct evidence for a G-quadruplex in a promoter region and its targeting with a small molecule to repress c-MYC transcription

5. Human telomeric G-quadruplex: The current status of telomeric G-quadruplexes as therapeutic targets in human cancer