Assessing the Structures and Interactions of γD-Crystallin Deamidation Variants.

ABSTRACT: Cataracts involve the deposition of the crystallin proteins in the vertebrate eye lens, causing opacification and blindness. They are associated with either genetic mutation or protein damage that accumulates over the lifetime of the organism. Deamidation of Asn residues in several different crystallins has been observed and is frequently invoked as a cause of cataract. Here, we investigated the properties of Asp variants, deamidation products of γD-crystallin, by solution NMR, X-ray crystallography, and other biophysical techniques. No substantive structural or stability changes were noted for all seven Asn to Asp γD-crystallins. Importantly, no changes in diffusion interaction behavior could be detected. Our combined experimental results demonstrate that introduction of single Asp residu

SUBMITTER: Guseman AJ 

PROVIDER: S-EPMC7935750 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature