Structural study of the G57W mutant of human gamma-S-crystallin, associated with congenital cataract.

ABSTRACT:

Purpose

Human γS-crystallin (CrygS) is an important component of the human eye lens nucleus and cortex. The mutation G57W in the molecule is reported to be associated with congenital cataract in children. We compare the conformational features and aggregation properties of the mutant protein G57W with the wild-type CrygS to understand how the structural changes in the mutant are related to the mechanism of opacification.

Methods

Wild-type and mutant proteins were cloned, expressed, and purified, and their structural properties were studied in solution. Conformational features and the structural stability of the proteins were compared in solution, using circular dichroism (CD) and fluorescence spectroscopic analysis, and the proteins' tendencies to aggregate were compared usi

SUBMITTER: Khan I 

PROVIDER: S-EPMC4943855 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature