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Annual Review of Physical Chemistry

Volume 72, 2021

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-crystallins are particularly amenable to structure determination by solid-state nuclear magnetic resonance (NMR) and solution NMR, as well as cryo-electron microscopy.

Keyword(s): intermolecular interactions, molecular chaperone, protein oligomer, protein solubility, vertebrate lens protein, α-crystallin
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2021-04-20
2024-04-16
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/content/journals/10.1146/annurev-physchem-090419-121428
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α-Crystallins in the Vertebrate Eye Lens: Complex Oligomers and Molecular Chaperones
Annual Review of Physical Chemistry 72, 143 (2021); https://doi.org/10.1146/annurev-physchem-090419-121428
/content/journals/10.1146/annurev-physchem-090419-121428
/content/journals/10.1146/annurev-physchem-090419-121428
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