Solution structure of a BolA-like protein from Mus musculus.

@article{Kasai2004SolutionSO,
  title={Solution structure of a BolA-like protein from Mus musculus.},
  author={Takuma Kasai and Makoto Inoue and Seizo Koshiba and Takashi Yabuki and Masaaki Aoki and Emi Nunokawa and Eiko Seki and Takayoshi Matsuda and Natsuko Matsuda and Yasuko Tomo and Mikako Shirouzu and Takaho Terada and Naomi Obayashi and Hiroaki Hamana and Naoko Shinya and Ayako Tatsuguchi and Satoko Yasuda and Mayumi Yoshida and Hiroshi Hirota and Y. Matsuo and Kazutoshi Tani and Harukazu Suzuki and Takahiro Arakawa and Piero Carninci and Jun Kawai and Yoshihide Hayashizaki and Takanori Kigawa and Shigeyuki Yokoyama},
  journal={Protein science : a publication of the Protein Society},
  year={2004},
  volume={13 2},
  pages={545-8}
}
The BolA-like proteins are widely conserved from prokaryotes to eukaryotes. The BolA-like proteins seem to be involved in cell proliferation or cell-cycle regulation, but the molecular function is still unknown. Here we determined the structure of a mouse BolA-like protein. The overall topology is alphabetabetaalphaalphabetaalpha, in which beta(1) and beta(2) are antiparallel, and beta(3) is parallel to beta(2). This fold is similar to the class II KH fold, except for the absence of the GXXG… CONTINUE READING

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