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Fig. 5. Computer analysis of the amino acid sequence of P68. (A) Results of potential coiled-coil domain search using COIL software. x-axis shows the amino acid residues starting from N-terminus, y-axis, the coiled-coil formation probability, P. (B) Computer alignment of human/mouse P68 (h/m P68) with mouse (mLB) and human (hLB) lamins B2 rod domain fragments. Potential coiled coils shown in A are boxed in yellow (P=0.62) and in orange rectangles (P>0.95). The green rectangle is coil 1A, the blue rectangle is coil 1B. The line below the alignment shows the similarity score: *, amino acids in that column are identical;:, conserved substitutions;., semi-conserved substitutions. The lines labelled p68 PrSS and LB PrSS represent prediction of the secondary structure of P68 and lamin B2, respectively, from its primary sequence. H, a region of {alpha}-helical structure; E, extended sheet; _ flexible coil structure.





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