Cataract-Causing S93R Mutant Destabilized Structural Conformation of βB1 Crystallin Linking With Aggregates Formation and Cellular Viability.

ABSTRACT: Cataract, opacity of the eye lens, is the leading cause of visual impairment worldwide. The crucial pathogenic factors that cause cataract are misfolding and aggregation of crystallin protein. βB1-crystallin, which is the most abundant water-soluble protein in mammalian lens, is essential for lens transparency. A previous study identified the missense mutation βB1-S93R being responsible for congenital cataract. However, the exact pathogenic mechanism causing cataract remains unclear. The S93 residue, which is located at the first Greek-key motif of βB1-crystallin, is highly conserved, and its substitution to Arginine severely impaired hydrogen bonds and structural conformation, which were evaluated via Molecular Dynamic Simulation. The βB1-S93R was also found to be prone to aggregat

SUBMITTER: Ren L 

PROVIDER: S-EPMC8964140 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature