A glimpse into the hidden world of the flexible C-terminal protein binding domains of human RAD52.
J Struct Biol
; 216(3): 108115, 2024 Sep.
Article
em En
| MEDLINE
| ID: mdl-39117045
ABSTRACT
Human RAD52 protein binds DNA and is involved in genomic stability maintenance and several forms of DNA repair, including homologous recombination and single-strand annealing. Despite its importance, there are very few structural details about the variability of the RAD52 ring size and the RAD52 C-terminal protein-protein interaction domains. Even recent attempts to employ cryogenic electron microscopy (cryoEM) methods on full-length yeast and human RAD52 do not reveal interpretable structures for the C-terminal half that contains the replication protein A (RPA) and RAD51 binding domains. In this study, we employed the monodisperse purification of two RAD52 deletion constructs and small angle X-ray scattering (SAXS) to construct a structural model that includes RAD52's RPA binding domain. This model is of interest to DNA repair specialists as well as for drug development against HR-deficient cancers.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Ligação Proteica
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Proteína Rad52 de Recombinação e Reparo de DNA
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Proteína de Replicação A
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Espalhamento a Baixo Ângulo
Limite:
Humans
Idioma:
En
Ano de publicação:
2024
Tipo de documento:
Article