title: XPD structure reveals its secrets.
abstract: The XPD protein is central to our understanding of the relationship between NER deficiencies and human disorders. Three recent papers report the crystal structures of XPD from archaea. Apart from anticipated helicase domains the structures reveal a 4FeS cluster and novel "Arch" domain. The structures help our understanding of genotype-phenotype relationships in the XPD gene.
authors.affiliation: Genome Damage and Stability Centre, University of Sussex, Falmer, Brighton, UK. a.r.lehmann@sussex.ac.uk
authors.forename: Alan R
authors.initials: AR
authors.lastname: Lehmann
mesh_terms: D001665:Binding Sites; D018360:Crystallography, X-Ray; D005838:Genotype; D006801:Humans; D008954:Models, Biological; D008957:Models, Genetic; D008958:Models, Molecular; D008968:Molecular Conformation; D009154:Mutation; D010641:Phenotype; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D016945:Sulfolobus acidocaldarius / Q000378:metabolism; D051759:Xeroderma Pigmentosum Group D Protein / Q000235:genetics* / Q000502:physiology*
chemical_list: D051759:Xeroderma Pigmentosum Group D Protein; C497292:ERCC2 protein, human