Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA.
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.
Ikegami
T
T
Graduate School of Biological Sciences, Nara Institute of Sciences and Technology, Ikoma, Japan.
Kuraoka
I
I
Saijo
M
M
Kodo
N
N
Kyogoku
Y
Y
Morikawa
K
K
Tanaka
K
K
Shirakawa
M
M
D000595:Amino Acid Sequence; D001665:Binding Sites; D004260:DNA Repair; D004268:DNA-Binding Proteins / Q000737:chemistry*; D006801:Humans; D008667:Metalloproteins / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D016601:RNA-Binding Proteins / Q000737:chemistry*; D051716:Replication Protein A; D017386:Sequence Homology, Amino Acid; D014983:Xeroderma Pigmentosum; D051760:Xeroderma Pigmentosum Group A Protein; D015032:Zinc
D004268:DNA-Binding Proteins; D008667:Metalloproteins; D016601:RNA-Binding Proteins; C497167:RPA1 protein, human; D051716:Replication Protein A; C497314:XPA protein, human; D051760:Xeroderma Pigmentosum Group A Protein; D015032:Zinc