Novel and Recurrent MYO7A Mutations in Usher Syndrome Type 1 and Type 2
Figure 4
Structural modeling of myosin-VIIa.
(A) Overview of the predicted structure of myosin-VIIa (3–769) covering the majority of the myosin head-like domain (1–729) and the first IQ motif (745–765). The ATP binding site (158–165) and the actin binding site (632–639) are included and are colored as red and green, respectively. The mutational spot identified in patient USH03-II:1 (Thr165) located in the ATP binding site is indicated in yellow. (B) A close view of the residue 165 highlighting the wide type amino acid threonine, the generated hydrogen bonds (in red), and their interacted amino acids, including Thr168, Lys169, Ser211, and Asp437. (C) Two previously indicated hydrogen bonds are eliminated due to the change of the wide type threonine into the mutant methionine.