Alpha-crystallin as a molecular chaperone.

摘要: The role of alpha-crystallin as a molecular chaperone may explain how the lens stays transparent for so long. Alpha-crystallin prevents aggregation other crystallins and proteins that have become unfolded by "trapping" protein in high weight complex. It also protects enzyme activities. substrate interact while molten globule state. predominantly binds to very early denaturation pathways. amphiphilic nature alpha-crystallin, polar C-terminal-region hydrophobic N-terminal-region are all essential function. flexible C-terminal extension maintains solubility can bind opposing charged residues unfolding proteins. Hydrophobic regions N-terminal region then hold protein. Specific areas important binding function been identified throughout N-terminal-region, connecting peptide extension. After substantial amount chemical data models, cryo-EM images confirmed variable 3D surface with hollow interior. taken from nucleus shows an age-dependent decrease High aggregates found within clear cataract lenses reduced Post-translational modifications, known occur during ageing, such glycation, carbamylation, oxidation, phosphorylation truncation cause is expressed outside lens. AlphaB-crystallin be induced heat shock many tissues where it translocated cytoplasm nucleus. Increased expression alphaB-crystallin has seen pathological states. Conformational disorders, including common aetiology potentially therapy.