Dissecting the contributions of β-hairpin tyrosine pairs to the folding and stability of long-lived human γD-crystallins.

ABSTRACT: Ultraviolet-radiation-induced damage to and aggregation of human lens crystallin proteins are thought to be a significant pathway to age-related cataract. The aromatic residues within the duplicated Greek key domains of γ- and β-crystallins are the main ultraviolet absorbers and are susceptible to direct and indirect ultraviolet damage. The previous site-directed mutagenesis studies have revealed a striking difference for two highly conserved homologous β-hairpin Tyr pairs, at the N-terminal domain (N-td) and C-terminal domain (C-td), respectively, in their contribution to the overall stability of HγD-Crys, but why they behave so differently still remains a mystery. In this paper, we systematically investigated the underlying molecular mechanism and detailed contributions of these two Tyr

SUBMITTER: Yang Z 

PROVIDER: S-EPMC3976203 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature