Figure 1
From: X-ray structure of engineered human Aortic Preferentially Expressed Protein-1 (APEG-1)
![Figure 1](http://media.springernature.com/full/springer-static/image/art%3A10.1186%2F1472-6807-5-21/MediaObjects/12900_2005_Article_54_Fig1_HTML.jpg)
Structure and sequence alignment of APEG-1. A: Alignment of APEG-1 with the I1 domain of titin (PDB 1G1C) and the telokin domain of MLCK (PDB 1FHG). The β-strands are labeled according to Ig fold I set nomenclature. The N-terminal 14 residues and the adhesion recognition RGD motif are highlighted. B: Ribbon diagram of the ΔAPEG-1 monomer. The front sheet (strands A'GFCC') and back sheet (strands ABED), are colored purple and pink, respectively. The 310 helix is shown in orange.