[Comparison on molecular characteristics of human gamma D-crystallin protein and its five mutations]

To gain further information on the mechanisms underling the cataractogenesis by bioinformatics analysis on molecular characteristics of gamma D-crystallin (CRYGD) protein and its five cataract-associated mutations.

With the analyzing software in bioinformatics website, we analyzed the (R14C, P23T, human wild-type CRYGD protein and the five reported mutations R36S, R58H and W156X), focusing on their physical-chemical characteristics, epitopes, post-translational modification sites, functional domains, secondary and tertiary structure.

R14C, R36S, R58H and W156X mutations resulted in a decrease in isoelectric point. R14C brought about a new cysteine residue exposed on the molecular surface. A decrease in local charge and a rise in local hydrophobicity was found in R14C, R36S and R58H. Local flexibility increased in P23T, while R58H caused a fall in local temperature.

The mutations were shown to cause changes in protein surface polarity, hydrophobicity, and spatial structure, contributing to protein deposition and cataract formation.