small acidic domain of Xeroderma pigmentosum group C complementing protein and similar proteins
This model represents the small acidic domain of mammalian Xeroderma pigmentosum group C complementing protein (XPC), yeast Rad4, and similar proteins. XPC/Rad4 recruits transcription/repair factor IIH (TFIIH) to the nucleotide excision repair (NER) complex through interactions with its p62/Tfb1 and XPB/Ssl2 TFIIH subunits. Global genome repair (GGR), one of two NER initiation pathways in mammals, starts with DNA lesion detection by XPC. XPC is a structure specific DNA-binding factor that recognizes distortion of the damaged DNA double helix and recruits the TFIIH complex onto the lesion to open up the damaged DNA. The small acidic domain of XPC/Rad4 interacts with the pleckstrin homology (PH) domain of the p62/Tfb1 subunit of TFIIH.