6WCY

N160D Deamidation Mutant of Human gammaD-Crystallin

Summary for 6WCY

• Entry DOI: 10.2210/pdb6wcy/pdb
• Related: 6W5B
• Descriptor: Gamma-crystallin D, SULFATE ION (3 entities in total)
• Functional Keywords: deamidation, lens, cataract, protein modification, aging, structural protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 41367.97

Authors

Whitley, M.J.,Rathi, N.,Ambarian, M.,Gronenborn, A.M. (deposition date: 2020-03-31, release date: 2021-01-20, Last modification date: 2023-10-18)

Primary citation

Guseman, A.J.,Whitley, M.J.,Gonzalez, J.J.,Rathi, N.,Ambarian, M.,Gronenborn, A.M.
Assessing the Structures and Interactions of gamma D-Crystallin Deamidation Variants.
Structure, 29:284-291.e3, 2021

PubMed 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 residues on the surface of γD-crystallin by deamidation is unlikely to be the driver of cataract formation in the eye lens.

PubMed: 33264606
DOI: 10.1016/j.str.2020.11.006

Experimental method

X-RAY DIFFRACTION (1.204 Å)