Supplementary Figure 6: Homology modeling of the MMP21 peptidase domain and amino acids substituted in patients with heterotaxy.
From: MMP21 is mutated in human heterotaxy and is required for normal left-right asymmetry in vertebrates
The MMP21 model is based on the MMP11 crystal structure. The upper and lower panels are views of the model rotated approximately 180° around the vertical axis with respect to one another. The peptidase domain of MMPs forms a spherical topology consisting of three α helices and a five-stranded β sheet (Biochim. Biophys. Acta 1803, 20–28, 2010), colored here in blue (helices) and orange (β strands). Residues affected in patients with heterotaxy (Glu215, Ile226 and Ala321) are colored magenta. Predicted hydrogen bonds involving these three residues are indicated as green lines. The side chain of Glu215 is predicted to form a hydrogen bond with the side chain of Arg195 (the latter is in blue).
