Structural modeling of myosin-VIIa.
figure
posted on 2014-05-15, 03:20 authored by Weining Rong, Xue Chen, Kanxing Zhao, Yani Liu, Xiaoxing Liu, Shaoping Ha, Wenzhou Liu, Xiaoli Kang, Xunlun Sheng, Chen Zhao(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.
