Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins

@inproceedings{NmethPongrcz2007FlexibleSM,
  title={Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins},
  author={Veronika N{\'e}meth-Pongr{\'a}cz and Orsolya Barab{\'a}s and M{\'o}nika Fuxreiter and Istv{\'a}n Simon and Iva Pichov{\'a} and Michalea Rumlov{\'a} and Helena Z{\'a}bransk{\'a} and Dmitri Svergun and Maxim V. Petoukhov and Veronika Harmat and {\'E}va Klement and {\'E}va Hunyadi-Guly{\'a}s and Katalin F Medzihradszky and Emese K{\'o}nya and Be{\'a}ta G. V{\'e}rtessy},
  booktitle={Nucleic acids research},
  year={2007}
}
The homotrimeric fusion protein nucleocapsid (NC)-dUTPase combines domains that participate in RNA/DNA folding, reverse transcription, and DNA repair in Mason-Pfizer monkey betaretrovirus infected cells. The structural organization of the fusion protein remained obscured by the N- and C-terminal flexible segments of dUTPase and the linker region connecting the two domains that are invisible in electron density maps. Small-angle X-ray scattering reveals that upon oligonucleotide binding the NC… CONTINUE READING

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