α-Crystallins Are Small Heat Shock Proteins: Functional and Structural Properties.
During its life cycle, a cell can be subjected to various external negative effects. Many proteins provide cell protection, including small heat shock proteins (sHsp) that have chaperone-like activity. These proteins have several important functions involving prevention of apoptosis and retention of cytoskeletal integrity; also, sHsp take part in the recovery of enzyme activity. The action mechanism of sHsp is based on the binding of hydrophobic regions exposed to the surface of a molten globule. α-Crystallins presented in chordate cells as two αA- and αB-isoforms are the most studied small heat shock proteins. In this review, we describe the main functions of α-crystallins, features of their secondary and tertiary structures, and examples of their partners in protein-protein interactions.
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia. ogalzit@vega.protres.ru.
T S
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Tikhomirova
O M
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Selivanova
O V
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Galzitskaya
D000818:Animals; D017209:Apoptosis / Q000502:physiology; D003599:Cytoskeleton / Q000737:chemistry / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D000072417:Protein Domains; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship; D038202:alpha-Crystallin A Chain / Q000737:chemistry* / Q000378:metabolism; D038203:alpha-Crystallin B Chain / Q000737:chemistry* / Q000378:metabolism
D006360:Heat-Shock Proteins; D038202:alpha-Crystallin A Chain; D038203:alpha-Crystallin B Chain