Crystal structure of the winged-helix domain of MCM8
| Autor: | Jun Li, Huan Zeng, Huiqin Xu, Huanhuan Li, Yingfang Liu |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Models Molecular Biophysics Winged Helix Crystallography X-Ray Biochemistry DNA-binding protein 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Minichromosome maintenance Protein Domains Humans Amino Acid Sequence Molecular Biology MCM8 biology Minichromosome Maintenance Proteins RecQ Helicases Chemistry Helicase Cell Biology DNA Cell biology 030104 developmental biology HEK293 Cells 030220 oncology & carcinogenesis biology.protein Homologous recombination Function (biology) Protein Binding |
| Zdroj: | Biochemical and biophysical research communications. 526(4) |
| ISSN: | 1090-2104 |
| Popis: | Minichromosome maintenance 8 (MCM8) is a recently identified member of the minichromosome maintenance family, which possesses helicase and ATPase activity. It interacts with MCM9 and participates in homologous recombination repair. The structure of MCM8 is unclear now. Here, we report the crystal structure of the winged-helix domain of human MCM8 (MCM8-WHD) at 1.21 A resolution. MCM8-WHD adopts a conserved winged-helix architecture. Structure analysis and biochemical study results showed the DNA binding ability and crucial residues of MCM8-WHD. Our results are helpful to understand the function of MCM8. |
| Databáze: | OpenAIRE |
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