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Making the Bend: DNA Tertiary Structure and Protein-DNA Interactions
DNA structure functions as an overlapping code to the DNA sequence. Rapid progress in understanding the role of DNA structure in gene regulation, DNA damage recognition and genome stability has been made. The three dimensional structure of both proteins and DNA plays a crucial role for their specifi...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4139847/ https://www.ncbi.nlm.nih.gov/pubmed/25026169 http://dx.doi.org/10.3390/ijms150712335 |
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author | Harteis, Sabrina Schneider, Sabine |
author_facet | Harteis, Sabrina Schneider, Sabine |
author_sort | Harteis, Sabrina |
collection | PubMed |
description | DNA structure functions as an overlapping code to the DNA sequence. Rapid progress in understanding the role of DNA structure in gene regulation, DNA damage recognition and genome stability has been made. The three dimensional structure of both proteins and DNA plays a crucial role for their specific interaction, and proteins can recognise the chemical signature of DNA sequence (“base readout”) as well as the intrinsic DNA structure (“shape recognition”). These recognition mechanisms do not exist in isolation but, depending on the individual interaction partners, are combined to various extents. Driving force for the interaction between protein and DNA remain the unique thermodynamics of each individual DNA-protein pair. In this review we focus on the structures and conformations adopted by DNA, both influenced by and influencing the specific interaction with the corresponding protein binding partner, as well as their underlying thermodynamics. |
format | Online Article Text |
id | pubmed-4139847 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-41398472014-08-21 Making the Bend: DNA Tertiary Structure and Protein-DNA Interactions Harteis, Sabrina Schneider, Sabine Int J Mol Sci Review DNA structure functions as an overlapping code to the DNA sequence. Rapid progress in understanding the role of DNA structure in gene regulation, DNA damage recognition and genome stability has been made. The three dimensional structure of both proteins and DNA plays a crucial role for their specific interaction, and proteins can recognise the chemical signature of DNA sequence (“base readout”) as well as the intrinsic DNA structure (“shape recognition”). These recognition mechanisms do not exist in isolation but, depending on the individual interaction partners, are combined to various extents. Driving force for the interaction between protein and DNA remain the unique thermodynamics of each individual DNA-protein pair. In this review we focus on the structures and conformations adopted by DNA, both influenced by and influencing the specific interaction with the corresponding protein binding partner, as well as their underlying thermodynamics. MDPI 2014-07-14 /pmc/articles/PMC4139847/ /pubmed/25026169 http://dx.doi.org/10.3390/ijms150712335 Text en © 2014 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Review Harteis, Sabrina Schneider, Sabine Making the Bend: DNA Tertiary Structure and Protein-DNA Interactions |
title | Making the Bend: DNA Tertiary Structure and Protein-DNA Interactions |
title_full | Making the Bend: DNA Tertiary Structure and Protein-DNA Interactions |
title_fullStr | Making the Bend: DNA Tertiary Structure and Protein-DNA Interactions |
title_full_unstemmed | Making the Bend: DNA Tertiary Structure and Protein-DNA Interactions |
title_short | Making the Bend: DNA Tertiary Structure and Protein-DNA Interactions |
title_sort | making the bend: dna tertiary structure and protein-dna interactions |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4139847/ https://www.ncbi.nlm.nih.gov/pubmed/25026169 http://dx.doi.org/10.3390/ijms150712335 |
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