Structural biology of multicomponent assemblies in DNA double-strand-break repair through non-homologous end joining.

Amanda K Chaplin, Tom L Blundell

Journal: Current opinion in structural biology 2021;61():9-16

PMID: 31733599

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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.

Address: Department of Biochemistry, University of Cambridge, CB2 1GA, Cambridge, United Kingdom.; Department of Biochemistry, University of Cambridge, CB2 1GA, Cambridge, United Kingdom. Electronic address: [email protected].

DOI: 10.1016/j.sbi.2019.09.008

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MeSH Terms: 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