The mutation V42M distorts the compact packing of the human gamma-S-crystallin molecule, resulting in congenital cataract.

ABSTRACT:

Background

Human γS-crystallin is an important component of the human eye lens nucleus and cortex. The mutation V42M in the molecule causes severe congenital cataract in children. We compare the structure of the mutant protein with that of the wild type in order to understand how structural changes in the mutant relate to the mechanism of opacification.

Methods

Both proteins were made using conventional cloning and expression procedures. Secondary and tertiary structural features of the proteins were analyzed using spectral methods. Structural stabilities of the proteins were analyzed using chemical and thermal denaturation methods. Self-aggregation was monitored using extrinsic spectral probes. Molecular modeling was used to compare the structural features of the two protei

SUBMITTER: Vendra VP 

PROVIDER: S-EPMC3528740 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature