Structural biology of multicomponent assemblies in DNA double-strand-break repair through non-homologous end joining.
Accepted version
Peer-reviewed
Repository URI
Repository DOI
Change log
Authors
Chaplin, Amanda K
Blundell, Tom L
Abstract
The mechanisms mediating the repair of DNA damage in human cells have been the focus of a multitude of studies since the middle of the previous century, and many of the proteins implicated in these processes have been identified as being part of large macromolecular assemblies. This review gives an overview of the current knowledge of protein structures specifically involved in the repair of DNA double strand breaks through Non-Homologous End Joining, with a focus on recent structures obtained via cryo-electron microscopy and prospects for how this rapidly evolving method will impact our understanding of DNA repair.
Description
Keywords
Amino Acid Motifs, Binding Sites, Cryoelectron Microscopy, Crystallography, X-Ray, DNA, DNA Breaks, Double-Stranded, DNA End-Joining Repair, DNA-Binding Proteins, Humans, Models, Molecular, Nucleic Acid Conformation, Structure-Activity Relationship
Journal Title
Curr Opin Struct Biol
Conference Name
Journal ISSN
0959-440X
1879-033X
1879-033X
Volume Title
61
Publisher
Elsevier BV
Publisher DOI
Sponsorship
Wellcome Trust (200814/Z/16/Z)
Wellcome Trust for a Programme Grant (O93167/Z/10/Z; 2011–2016) and Investigator Award (200814/Z/16/Z; 2016 -)