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Your search keyword '"Hamana, Hiroaki"' showing total 8 results
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8 results on '"Hamana, Hiroaki"'

6. Crystal structure of the conserved protein TT1542 from Thermus thermophilus HB8

Author

Handa, Noriko, primary, Terada, Takaho, additional, Kamewari, Yuki, additional, Hamana, Hiroaki, additional, Tame, Jeremy R.H., additional, Park, Sam‐Yong, additional, Kinoshita, Kengo, additional, Ota, Motonori, additional, Nakamura, Haruki, additional, Kuramitsu, Seiki, additional, Shirouzu, Mikako, additional, and Yokoyama, Shigeyuki, additional

Published
2003
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7. Solution structure of a BolA-like protein from Mus musculus.

Author

Kasai, Takuma, Inoue, Makoto, Koshiba, Seizo, Yabuki, Takashi, Aoki, Masaaki, Nunokawa, Emi, Seki, Eiko, Matsuda, Takayoshi, Matsuda, Natsuko, Tomo, Yasuko, Shirouzu, Mikako, Terada, Takaho, Obayashi, Naomi, Hamana, Hiroaki, Shinya, Naoko, Tatsuguchi, Ayako, Yasuda, Satoko, Yoshida, Mayumi, Hirota, Hiroshi, and Matsuo, Yo

Abstract

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 αββααβα, in which β1 and β2 are antiparallel, and β3 is parallel to β2. This fold is similar to the class II KH fold, except for the absence of the GXXG loop, which is well conserved in the KH fold. The conserved residues in the BolA-like proteins are assembled on the one side of the protein. [ABSTRACT FROM AUTHOR]

Published
2004
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8. Solution structure of a BolA-like protein from Mus musculus.

Author

Kasai T, Inoue M, Koshiba S, Yabuki T, Aoki M, Nunokawa E, Seki E, Matsuda T, Matsuda N, Tomo Y, Shirouzu M, Terada T, Obayashi N, Hamana H, Shinya N, Tatsuguchi A, Yasuda S, Yoshida M, Hirota H, Matsuo Y, Tani K, Suzuki H, Arakawa T, Carninci P, Kawai J, Hayashizaki Y, Kigawa T, and Yokoyama S

Subjects
Amino Acid Sequence, Animals, Humans, Mice, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary, Sequence Homology, Amino Acid, Solutions chemistry, Nuclear Magnetic Resonance, Biomolecular, Proteins chemistry
Abstract

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 loop, which is well conserved in the KH fold. The conserved residues in the BolA-like proteins are assembled on the one side of the protein.

Published
2004
Full Text
View/download PDF

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