The redefined DNA-binding domain of human xeroderma pigmentosum complementation group A: production, crystallization and structure solution.

ABSTRACT: Human xeroderma pigmentosum complementation group A (XPA) is a scaffold protein that plays significant roles in DNA-damage verification and in recruiting downstream endonucleases to facilitate the repair of DNA lesions in nucleotide-excision repair. XPA_98-219 (residues 98-219) has been identified as a DNA-binding domain and has been extensively studied in the last two decades. However, the most recent studies have redefined the DNA-binding domain as XPA_98-239 (residues 98-239); it exerts a remarkably higher DNA-binding affinity than XPA_98-219 and has a binding affinity that is quite similar to that of the full-length protein. Here, the production, crystallization and structure solution of human XPA_98-239 are described. Crystals were obtained usin

SUBMITTER: Lian FM 

PROVIDER: S-EPMC6317461 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature