Figure 1
From: Rare deleterious mutations of the gene EFR3A in autism spectrum disorders
Ribbon diagram of S. cerevisiae Efr3 crystal structure. Crystallization of Efr3 revealed a series of HEAT repeats, as we had predicted bioinformatically. Alignment of yeast Efr3 and human EFR3A was reliable to amino acid 451. Blinded to case/control status, the human mutations were mapped and analyzed for their potential to disrupt protein structure and function given the three-dimensional crystal structure. Mutations in red are deleterious and found in cases. (R161* in a control and G216Sfs*12 in a case are not shown but presumed to be deleterious.) Mutations in green are benign and found in cases. Mutations in blue are benign and found in controls.