Figure 5.

(A) Schematic putative arrangement of a normal fibulin 5 cbEGF that is based on the UniProt sequence for fibulin 5¹⁵ and the consensus sequence for class I cbEGFs,²⁹ and that could represent each of fibulin 5 cbEGF-2 to -6, but not the abnormal cbEGF 1. Disulfide bonds are shown in red. Conserved residues are labeled using one-letter abbreviations. The positions of mutations associated with cutis laxa and AMD that lay within fibulin 5 cbEGFs 2 to 6 are shown on this representation of a single cbEGF. (B, C) Swiss-Model³¹ used the alignments produced by threading (Supplementary Fig. S3) to generate (B) an alignment of peptide backbones for fibulin 5 cbEGF-4 (green) and fibrillin 1 cbEGF 33 (blue) and therefore (C) a putative homology model for fibulin 5 WT cbEGF 4. Cysteines and disulfide bonds are shown in red with the exceptions of residue C217 (yellow) and the disulfide bond (not shown) that is broken with the C217R mutation. Blue: the position of S227.