Deamidation of the human eye lens protein γS-crystallin accelerates oxidative aging
B. Norton-Baker, P. Mehrabi, A. O. Kwok, K. W. Roskamp, M. A. Spague-Piercy, D. von Stetten, R. J. D. Miller, R. W. Martin
This study reports six crystal structures of deamidated γS-crystallin variants, showing increased instability, aggregation, and disulfide bond formation, suggesting deamidation accelerates oxidative aging in the human lens.
Structure · May 1, 2022Peer-reviewedBiochemistry