{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T09:16:33Z","timestamp":1788426993621,"version":"build-2803163510"},"reference-count":26,"publisher":"American Chemical Society (ACS)","issue":"31","license":[{"start":{"date-parts":[[2015,7,21]],"date-time":"2015-07-21T00:00:00Z","timestamp":1437436800000},"content-version":"vor","delay-in-days":365,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_termsofuse.html"}],"funder":[{"DOI":"10.13039\/100000054","name":"National Cancer Institute","doi-asserted-by":"publisher","award":["PO1 CA092584"],"award-info":[{"award-number":["PO1 CA092584"]}],"id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000066","name":"National Institute of Environmental Health Sciences","doi-asserted-by":"publisher","award":["R01 ES1065561"],"award-info":[{"award-number":["R01 ES1065561"]}],"id":[{"id":"10.13039\/100000066","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000097","name":"National Center for Research Resources","doi-asserted-by":"publisher","award":["S10 RR025677"],"award-info":[{"award-number":["S10 RR025677"]}],"id":[{"id":"10.13039\/100000097","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000153","name":"Division of Biological Infrastructure","doi-asserted-by":"publisher","award":["DBI-0922862"],"award-info":[{"award-number":["DBI-0922862"]}],"id":[{"id":"10.13039\/100000153","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2014,8,6]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Xeroderma pigmentosum complementation group A (XPA) protein plays a critical role in the repair of DNA damage via the nucleotide excision repair (NER) pathway. XPA serves as a scaffold for NER, interacting with several other NER proteins as well as the DNA substrate. The critical importance of XPA is underscored by its association with the most severe clinical phenotypes of the genetic disorder Xeroderma pigmentosum. Many of these disease-associated mutations map to the XPA98\u2013219 DNA-binding domain (DBD) first reported \u223c20 years ago. Although multiple solution NMR structures of XPA98\u2013219 have been determined, the molecular basis for the interaction of this domain with DNA is only poorly characterized. In this report, we demonstrate using a fluorescence anisotropy DNA-binding assay that the previously reported XPA DBD binds DNA with substantially weaker affinity than the full-length protein. In-depth analysis of the XPA sequence suggested that the original DBD construct lacks critical basic charge and helical elements at its C-terminus. Generation and analysis of a series of C-terminal extensions beyond residue 219 yielded a stable, soluble human XPA98\u2013239 construct that binds to a Y-shaped ssDNA\u2013dsDNA junction and other substrates with the same affinity as the full-length protein. Two-dimensional 15N\u20131H NMR suggested XPA98\u2013239 contains the same globular core as XPA98\u2013219 and likely undergoes a conformational change upon binding DNA. Together, our results demonstrate that the XPA DBD should be redefined and that XPA98\u2013239 is a suitable model to examine the DNA binding activity of human XPA.<\/jats:p>","DOI":"10.1021\/ja503020f","type":"journal-article","created":{"date-parts":[[2014,7,21]],"date-time":"2014-07-21T11:53:07Z","timestamp":1405943587000},"page":"10830-10833","source":"Crossref","is-referenced-by-count":41,"title":["Redefining\nthe DNA-Binding Domain of Human XPA"],"prefix":"10.1021","volume":"136","author":[{"given":"Norie","family":"Sugitani","sequence":"first","affiliation":[{"name":"Vanderbilt University , , , ,","place":["Nashville, Tennessee, United States, 37232-8725"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steven M.","family":"Shell","sequence":"additional","affiliation":[{"name":"Vanderbilt University , , , ,","place":["Nashville, Tennessee, United States, 37232-8725"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarah E.","family":"Soss","sequence":"additional","affiliation":[{"name":"Vanderbilt University , , , ,","place":["Nashville, Tennessee, United States, 37232-8725"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Walter J.","family":"Chazin","sequence":"additional","affiliation":[{"name":"Vanderbilt University , , , ,","place":["Nashville, Tennessee, United States, 37232-8725"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2014,7,21]]},"reference":[{"key":"2026090304404893000_cit1","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1021\/cr040483f","volume":"106","author":"Gillet","year":"2006","journal-title":"Chem. 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