{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,4]],"date-time":"2026-08-04T20:35:26Z","timestamp":1785875726574,"version":"3.56.0"},"reference-count":0,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2003,10,30]],"date-time":"2003-10-30T00:00:00Z","timestamp":1067472000000},"content-version":"vor","delay-in-days":2738,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Genes to Cells"],"published-print":{"date-parts":[[1996,5]]},"abstract":"<jats:p> <jats:italic>Background<\/jats:italic>: The XPA (xeroderma pigmentosum group A) protein specifically recognizes the UV\u2010 or chemically damaged DNA lesions, and triggers the nucleotide excision repair process. This XPA protein contains the functional domain which is crucial to the recognition of damaged DNA. Its primary structure suggests that this DNA binding domain may contain a zinc\u2010finger motif. To gain a more detailed insight into this zinc\u2010finger motif, we have measured the <jats:sup>113<\/jats:sup>Cd\u2010NMR spectra of the DNA binding domains derived from the wild\u2010type and mutant XPA proteins.<\/jats:p><jats:p> <jats:italic>Results<\/jats:italic>:\u2002<jats:sup>113<\/jats:sup>Cd\u2010NMR analysis, combined with atomic absorption and site\u2010directed mutagenesis, revealed that the DNA binding domain contains one zinc ion, coordinated with four cysteine residues (Cys105, Cys108, Cys126, and Cys129), that is essential for correct protein folding <jats:italic>in vivo<\/jats:italic> and <jats:italic>in vitro<\/jats:italic><\/jats:p><jats:p> <jats:italic>Conclusions<\/jats:italic>:\u2002The four ligand cysteine residues form a Cys\u2010X<jats:sub>2<\/jats:sub>\u2010Cys\u2010X<jats:sub>17<\/jats:sub>\u2010Cys\u2010X<jats:sub>2<\/jats:sub>\u2010Cys motif, which is reminiscent of the (Cys)<jats:sub>4<\/jats:sub> type zinc\u2010finger motif found in numerous transcriptional regulatory proteins. However, the secondary structure prediction and the 3D\u20101D compatibility analysis demonstrate that there is no structural similarity in the vicinity of the zinc\u2010finger motif between the XPA protein and other zinc\u2010finger containing proteins. We conclude that the XPA protein contains a new type of zinc\u2010finger motif.<\/jats:p>","DOI":"10.1046\/j.1365-2443.1996.d01-252.x","type":"journal-article","created":{"date-parts":[[2003,11,2]],"date-time":"2003-11-02T14:57:05Z","timestamp":1067785025000},"page":"437-442","source":"Crossref","is-referenced-by-count":33,"title":["<b>Implications of the zinc\u2010finger motif found in the DNA\u2010binding domain of the human XPA protein<\/b>"],"prefix":"10.1111","volume":"1","author":[{"given":"Eugene H.","family":"Morita","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tadayasu","family":"Ohkubo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Isao","family":"Kuraoka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masahiro","family":"Shirakawa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kiyoji","family":"Tanaka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kosuke","family":"Morikawa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2003,10,30]]},"container-title":["Genes to Cells"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1046%2Fj.1365-2443.1996.d01-252.x","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1046\/j.1365-2443.1996.d01-252.x","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1046\/j.1365-2443.1996.d01-252.x","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,9,11]],"date-time":"2023-09-11T06:26:07Z","timestamp":1694413567000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1046\/j.1365-2443.1996.d01-252.x"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1996,5]]},"references-count":0,"journal-issue":{"issue":"5","published-print":{"date-parts":[[1996,5]]}},"alternative-id":["10.1046\/j.1365-2443.1996.d01-252.x"],"URL":"https:\/\/doi.org\/10.1046\/j.1365-2443.1996.d01-252.x","archive":["Portico"],"relation":{},"ISSN":["1356-9597","1365-2443"],"issn-type":[{"value":"1356-9597","type":"print"},{"value":"1365-2443","type":"electronic"}],"subject":[],"published":{"date-parts":[[1996,5]]}}}