IDR Logo

Please use this identifier to cite or link to this item:
Title: Differential role of arginine mutations on the structure and functions of ?-crystallin
Authors: Panda A.K.
Nandi S.K.
Chakraborty A.
Nagaraj R.H.
Biswas A.
Keywords: Arginine mutations
Congenital cataract
Post-translational modifications
Issue Date: 2016
Citation: 10
Abstract: Background ?-Crystallin is a major protein of the eye lens in vertebrates. It is composed of two subunits, ?A- and ?B-crystallin. ?-Crystallin is an oligomeric protein having these two subunits in 3:1 ratio. It belongs to small heat shock protein family and exhibits molecular chaperone function, which plays an important role in maintaining the lens transparency. Apart from chaperone function, both subunits also exhibit anti-apoptotic property. Comparison of their primary sequences reveals that ?A- and ?B-crystallin posses 13 and 14 arginine residues, respectively. Several of them undergo mutations which eventually lead to various eye diseases such as congenital cataract, juvenile cataract, and retinal degeneration. Interestingly, many arginine residues of these subunits are modified during glycation and even some are truncated during aging. All these facts indicate the importance of arginine residues in ?-crystallin. Scope of review In this review, we will emphasize the recent in vitro and in vivo findings related to congenital cataract causing arginine mutations in ?-crystallin. Major conclusions Congenital cataract causing arginine mutations alters the structure and decreases the chaperone function of ?-crystallin. These mutations also affect the lens morphology and phenotypes. Interestingly, non-natural arginine mutations (generated for mimicking the glycation and truncation environment) improve the chaperone function of ?-crystallin which may play an important role in maintaining the eye lens transparency during aging. General significance The neutralization of positive charge on the guanidino group of arginine residues is not always detrimental to the functionality of ?-crystallin. This article is part of a Special Issue entitled Crystallin Biochemistry in Health and Disease. � 2015 Elsevier B.V.
Appears in Collections:Research Publications

Files in This Item:
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.