In:
Biological Chemistry, Walter de Gruyter GmbH, Vol. 391, No. 7 ( 2010-07-01)
Abstract:
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.
Type of Medium:
Online Resource
ISSN:
1437-4315
,
1431-6730
Language:
Unknown
Publisher:
Walter de Gruyter GmbH
Publication Date:
2010
detail.hit.zdb_id:
1466062-3
SSG:
12
Permalink
