Assessing the Structures and Interactions of γD-Crystallin Deamidation Variants.
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ABSTRACT:
SUBMITTER: Guseman AJ
PROVIDER: S-EPMC7935750 | biostudies-literature | 2021 Mar
REPOSITORIES: biostudies-literature
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Assessing the Structures and Interactions of γD-Crystallin Deamidation Variants.
Guseman Alex J AJ Whitley Matthew J MJ González Jeremy J JJ Rathi Nityam N Ambarian Mikayla M Gronenborn Angela M AM
Structure (London, England : 1993) 20201201 3
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 crystallogr ...[more]
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