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1 RIKEN Genomic Sciences Center, Yokohama, Japan
2 Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, Tokyo, Japan
3 RIKEN Harima Institute at SPring-8, Hyogo, Japan
(RECEIVED September 1, 2003; FINAL REVISION September 1, 2003; ACCEPTED October 7, 2003)






, in which
1 and
2 are antiparallel, and
3 is parallel to
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. Keywords: NMR structure; conserved protein; BolA; cell proliferation; cell-cycle regulation; KH fold; structural genomics
Reprint requests to: Shigeyuki Yokoyama, Protein Research Group, RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan; e-mail: yokoyama{at}biochem.s.u-tokyo.ac.jp; fax: 81-45-503-9195.
Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03401004.
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