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The N-terminus of FILIA Forms an Atypical KH Domain with a Unique Extension Involved in Interaction with RNA

Figure 1

The structure of FILIA-N.

(A) Overall structure of FILIA-N. Molecule is shown colored from blue at the N-terminus to red at the C-terminus, and secondary structure elements are labeled. (B) Superimposition of FILIA-N (monomer1) and Nova2-KH3. FILIA-N is colored green from residues 40–117, and pale green from residues 2–39; Nova2-KH3 is shown in yellow. (C) Sequence alignment for members of the oocyte/embryo expressed gene family by ClustalW [60]. All sequences are from mouse, and only the N-terminal KH region is shown. The number following the sequence in parentheses refers to the number of remaining residues in the variable C-terminus of the protein. Residues are colored according to their characteristics, i.e., red for hydrophobic, green for polar, blue for negatively charged and purple for positively charged. Invariant residues are shown with brown background, and conserved residues are shown with yellow background. Secondary structure elements are labeled on top of the alignment, as in Fig. 1A.

Figure 1

doi: https://doi.org/10.1371/journal.pone.0030209.g001