A structural bioinformatics investigation on protein–DNA complexes delineates their modes of interaction-Reference-Cited by-同舟云学术

A structural bioinformatics investigation on protein–DNA complexes delineates their modes of interaction

Published:2017 Issue:5 Volume:13 Page:1010-1017
ISSN:1742-206X
Container-title:Molecular BioSystems
language:en
Short-container-title:Mol. BioSyst.

Author:

Gardini Simone¹²³⁴,Furini Simone⁵³⁶⁴,Santucci Annalisa¹²³⁴,Niccolai Neri¹²³⁴^ORCID

Affiliation:

1. Department of Biotechnology

2. Chemistry and Pharmacy

3. University of Siena

4. Italy

5. Department of Medical Biotechnologies

6. Siena

Abstract

A non-redundant dataset of 629 protein–DNA complexes has been used to investigate on amino acid composition of protein-DNA interfaces. Structural proteins, transcription factors and DNA-related enzymes show specific patterns accounting for different modes of their interaction with DNA.

Publisher

Royal Society of Chemistry (RSC)

Subject

Molecular Biology,Biotechnology

Link

http://pubs.rsc.org/en/content/articlepdf/2017/MB/C7MB00071E

Reference57 articles.

1. A structural taxonomy of DNA-binding domains

2. Bioinformatic analysis of the protein/DNA interface

3. Protein–DNA Interactions: Amino Acid Conservation and the Effects of Mutations on Binding Specificity

4. Amino acid-base interactions: a three-dimensional analysis of protein-DNA interactions at an atomic level

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