Fig. 3.

Sequence alignment and homology models of the tenascin family FBG domains. a Multiple alignment analysis of the FBG domain of tenascin family members highlighting the secondary structure of the predicted protein models. Blue line indicates the A-subdomain, red line indicates the B-subdomain, and yellow line indicates the P-subdomain. The alignment was colored according to the Clustal color scheme. Light blue: hydrophobic, red: positive charged, green: polar, pink: conserved column of cysteine, violet: negative charged, orange: glycine, yellow: proline, cyan: aromatics. The overlapping sequence of peptides 5 and 6, the sequence of peptide 7, and the C terminus are indicated with purple, black, and gray boxes, respectively. b Homology models of the FBG domain of tenascin-C, -R, -W, and -X highlighting the amino acid composition in loop 5, loop 7, and loop 10. The sequence of loop 5 is depicted in pale orange, within which positively charged residues are colored red, any positive residues in the C-terminal loop 10 are also colored red. The sequence of loop 7 is colored pale green within which the triad of polar and hydrophobic residues conserved in FBG-C, -R, and -W but absent in FBG-X, are colored purple, dark green, and blue