Solution structure of a BolA-like protein from Mus musculus
| Autor: | Naoko Shinya, Masaaki Aoki, Takaho Terada, Takayoshi Matsuda, Satoko Yasuda, Yoshihide Hayashizaki, Mayumi Yoshida, Jun Kawai, Takashi Yabuki, Takahiro Arakawa, Mikako Shirouzu, Hiroaki Hamana, Natsuko Matsuda, Y. Matsuo, Takanori Kigawa, Piero Carninci, Seizo Koshiba, Emi Nunokawa, Yasuko Tomo, Eiko Seki, Shigeyuki Yokoyama, Kazutoshi Tani, Takuma Kasai, Makoto Inoue, Ayako Tatsuguchi, Hiroshi Hirota, Naomi Obayashi, Harukazu Suzuki |
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| Rok vydání: | 2004 |
| Předmět: |
Models
Molecular Globular protein Molecular Sequence Data Biology Thioredoxin fold Antiparallel (biochemistry) Biochemistry Protein Structure Secondary Structural genomics Mice Protein structure Animals Humans Amino Acid Sequence Nuclear Magnetic Resonance Biomolecular Molecular Biology Peptide sequence chemistry.chemical_classification Sequence Homology Amino Acid Proteins Globin fold Amino acid Solutions chemistry For the Record |
| Zdroj: | Protein Science. 13:545-548 |
| ISSN: | 1469-896X 0961-8368 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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