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Significant efforts are made to investigate NER since mutations in any of the seven XPps may cause the xeroderma pigmentosum and trichothiodystrophy diseases. However, these proteins collaborate with other pivotal players in all known NER steps to accurately exert their purposes. Therefore, in the old and ever\u2010evolving field of DNA repair, it is imperative to reexamine and describe their structures to understand NER properly. This work provides an up\u2010to\u2010date review of the protein structural aspects of the closest partners that directly interact and influence XPps: RAD23B, CETN2, DDB1, RPA (RPA70, 32, and 14), p8 (GTF2H5), and ERCC1. Structurally and functionally vital domains, regions, and critical residues are reexamined, providing structural lessons and perspectives about these indispensable proteins in the NER and other DNA repair pathways. By gathering all data related to the major human xeroderma pigmentosum\u2010interacting proteins, this review will aid newcomers on the subject and guide structural and functional future studies.<\/jats:p>","DOI":"10.1002\/pro.4173","type":"journal-article","created":{"date-parts":[[2021,8,22]],"date-time":"2021-08-22T06:44:10Z","timestamp":1629614650000},"page":"2187-2205","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["Every protagonist has a sidekick: Structural aspects of human xeroderma pigmentosum\u2010binding proteins in nucleotide excision repair"],"prefix":"10.1002","volume":"30","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2825-8295","authenticated-orcid":false,"given":"Bruno C\u00e9sar","family":"Feltes","sequence":"first","affiliation":[{"name":"Department of Theoretical Informatics, Institute of Informatics, Department of Theoretical Informatics Federal University of Rio Grande do Sul  Porto 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