Deamidation in human lens betaB2-crystallin destabilizes the dimer.

ABSTRACT: Two major determinants of the transparency of the lens are protein-protein interactions and stability of the crystallins, the structural proteins in the lens. betaB2 is the most abundant beta-crystallin in the human lens and is important in formation of the complex interactions of lens crystallins. betaB2 readily forms a homodimer in vitro, with interacting residues across the monomer-monomer interface conserved among beta-crystallins. Due to their long life spans, crystallins undergo an unusually large number of modifications, with deamidation being a major factor. In this study the effects of two potential deamidation sites at the monomer-monomer interface on dimer formation and stability were determined. Glutamic acid substitutions were constructed to mimic the effects of previously rep

SUBMITTER: Lampi KJ 

PROVIDER: S-EPMC2533042 | biostudies-literature | 2006 Mar

REPOSITORIES: biostudies-literature