Structure of the human FN monomer. (A) Modular structure
of FN protein emphasizing folding motifs, FN-I, FN-II, and FN-III.
(B) Secondary structures of selected FN-III modules with
accurate representations of relative β-strand lengths with respect to
each other. The upper sheets are shaded gray while lower sheets are
white. (C) Sequence alignment of the four FN-III
modules. FN-III7, FN-III8, FN-III9,
and FN-III10 have 93, 91, 91, and 94 aa, respectively. Key
residues discussed within the text are highlighted in dark gray, while
residues forming key hydrogen bonds are connected by arrows.