α-Crystallins in the Vertebrate Eye Lens: Complex Oligomers and Molecular Chaperones.

ABSTRACT: α-Crystallins are small heat-shock proteins that act as holdase chaperones. In humans, αA-crystallin is expressed only in the eye lens, while αB-crystallin is found in many tissues. α-Crystallins have a central domain flanked by flexible extensions and form dynamic, heterogeneous oligomers. Structural models show that both the C- and N-terminal extensions are important for controlling oligomerization through domain swapping. α-Crystallin prevents aggregation of damaged β- and γ-crystallins by binding to the client protein using a variety of binding modes. α-Crystallin chaperone activity can be compromised by mutation or posttranslational modifications, leading to protein aggregation and cataract. Because of their high solubility and their ability to form large, functional oligomers, α-crys

SUBMITTER: Sprague-Piercy MA 

PROVIDER: S-EPMC8062273 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature