Three-dimensional Structure of SOX Protein-DNA Complexes

Prasanna R. Kolatkar*, Balasubramanian Moovarkumudalvan, Essam M. Abdelalim, Mohamed M. Emara

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

2 Citations (Scopus)

Abstract

The SOX family of proteins has been studied at many levels, with the biggest impact coming from genomics, transcriptomics, and other high-throughput methods, that augment the large amount of functional biology studied to date. One of the key areas that are useful for understanding the mechanistic roles of this family is to study the structures of its members to gain mechanistic insights into how their partnerships with other proteins and binding to their genomic loci elicit the diverse set of cell developmental programs. However, the amount of structural biology information is relatively sparse compared to other "omics" technologies. This chapter will analyze all available SOX structures to date in terms of binding to other protein partners as well as to the cognate deoxyribonucleic acid and will summarize the functional consequences of the binding modes.

Original languageEnglish
Title of host publicationSox2
Subtitle of host publicationBiology and Role in Development and Disease
PublisherElsevier Inc.
Pages15-24
Number of pages10
ISBN (Electronic)9780128004203
ISBN (Print)9780128003527
DOIs
Publication statusPublished - 2016

Keywords

  • Crystallography
  • Development
  • ESC
  • HMG domain
  • IPSC
  • NMR
  • SOX
  • Stem cell
  • Structure

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