Nature Structural Biology
5, 701 - 706 (1998)
doi:10.1038/1400
Solution structure of the DNA- and RPA-binding domain of the human repair
factor XPATakahisa Ikegami1, Isao Kuraoka2, Masafumi Saijo2, Naohiko Kodo2, Yoshimasa Kyogoku3, Kosuke Morikawa4, Kiyoji Tanaka2
& Masahiro Shirakawa11
Graduate School of Biological Sciences, Nara Institute
of Science and Technology,8916-5 Takayama,Ikoma,
Nara
630-0101,Japan. 2
Institute for Molecular and Cellular Biology, Osaka
University, 1-3 Yamadaoka, Suita, Osaka
565, Japan. 3
Institute for Protein Research, Osaka University,
3-2 Yamadaoka, Suita, Osaka 565, Japan
. 4
Biomolecular Engineering Research Institute,
.6-2-3 Furuedai, Suita, Osaka 565, Japan
.
Correspondence should be addressed to Masahiro Shirakawa shira@bs.aist-nara.ac.jp
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  / structure with a positively
charged superficial cleft. From the NMR spectra of the complexes, DNA and
RPA binding surfaces are suggested.
|
