Rudolf Virchow Center for Experimental Biomedicine, Institute for Structural Biology, University of Würzburg, D-97080 Würzburg, Germany.
Biol Chem. 2010 Jul;391(7):761-5. doi: 10.1515/BC.2010.076.
Xeroderma pigmentosum complementation group D protein (XPD) is an iron-sulfur cluster containing 5'-3' helicase and, in humans, part of the transcription factor TFIIH. TFIIH is involved in nucleotide excision repair as well as in transcription initiation. Recently, three different groups have reported the structures of archaeal XPDs. All structures revealed a four-domain organization with two RecA-like domains, an Arch domain and an iron-sulfur cluster domain. It was possible to rationalize several of the mutations in the human XPD gene that lead to one of the three severe diseases xeroderma pigmentosum, Cockayne syndrome and trichothiodystrophy. The different structures are compared and disease-related mutations are discussed.
着色性干皮病互补组 D 蛋白 (XPD) 是一种含铁-硫簇的 5'-3'解旋酶,在人类中是转录因子 TFIIH 的一部分。TFIIH 参与核苷酸切除修复以及转录起始。最近,三个不同的小组报告了古细菌 XPD 的结构。所有结构都揭示了一个四结构域组织,包含两个 RecA 样结构域、一个 Arch 结构域和一个铁-硫簇结构域。可以对导致三种严重疾病(着色性干皮病、Cockayne 综合征和毛发硫营养不良症)之一的人类 XPD 基因突变进行合理化解释。比较了不同的结构,并讨论了与疾病相关的突变。