α-Crystallins are small heat shock proteins: Functional and structural properties
- Autores: Tikhomirova T.S.1,2, Selivanova O.M.1, Galzitskaya O.V.1
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Afiliações:
- Institute of Protein Research
- Institute for Biological Instrumentation
- Edição: Volume 82, Nº 2 (2017)
- Páginas: 106-121
- Seção: Review
- URL: https://journals.rcsi.science/0006-2979/article/view/151240
- DOI: https://doi.org/10.1134/S0006297917020031
- ID: 151240
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Resumo
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 αAand 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.
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Sobre autores
T. Tikhomirova
Institute of Protein Research; Institute for Biological Instrumentation
Email: ogalzit@vega.protres.ru
Rússia, Pushchino, Moscow Region, 142290; Pushchino, Moscow Region, 142290
O. Selivanova
Institute of Protein Research
Email: ogalzit@vega.protres.ru
Rússia, Pushchino, Moscow Region, 142290
O. Galzitskaya
Institute of Protein Research
Autor responsável pela correspondência
Email: ogalzit@vega.protres.ru
Rússia, Pushchino, Moscow Region, 142290
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