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.
Nat Struct Biol. 1998 Aug;5(8):701-6. doi: 10.1038/1400.
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.
人类核苷酸切除修复蛋白XPA的中央结构域可与受损DNA及复制蛋白A（RPA）结合，其溶液结构通过核磁共振（NMR）光谱法得以确定。中央结构域由一个含锌亚结构域和一个C端亚结构域组成。含锌亚结构域具有紧密的球状结构，与转录因子中的锌指结构不同。C端亚结构域折叠成一种具有带正电荷表面裂隙的新型α/β结构。从复合物的NMR光谱推测出了DNA和RPA的结合表面。
