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1: Nat Struct Biol. 1998 Aug;5(8):701-6.Click here to read Links

Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA.

Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M.

Graduate School of Biological Sciences, Nara Institute of Sciences and Technology, Ikoma, Japan.

The solution structure of the central domain of the human nucleotide excision repair protein XPA, which binds to damaged DNA and replication protein A (RPA), was determined by nuclear magnetic resonance (NMR) spectroscopy. The central domain consists of a zinc-containing subdomain and a C-terminal subdomain. The zinc-containing subdomain has a compact globular structure and is distinct from the zinc-fingers found in transcription factors. The C-terminal subdomain folds into a novel alpha/beta structure with a positively charged superficial cleft. From the NMR spectra of the complexes, DNA and RPA binding surfaces are suggested.

PMID: 9699634 [PubMed - indexed for MEDLINE]

Structures reported by this article