Structure and function of the small heat shock protein/α-crystallin family of molecular chaperones

Autor: Slingsby C, Vierling E, Van Montfort R
Rok vydání: 2001
Předmět:
Zdroj: Protein Folding in the Cell ISBN: 9780120342594
DOI: 10.1016/s0065-3233(01)59004-x
Popis: Publisher Summary The goal of this chapter is to clarify the diversity within the heat shock proteins (sHsps) family and to describe evidence indicating that sHsps have many different substrates and affect a wide range of cellular functions. The diversity of sHsp structure and expression patterns is immense, and their activities in vivo may involve multiple mechanisms. The sHsps and the structurally related vertebrate eye lens α-crystallins are the poor cousins in the family of molecular chaperones, and remain the least understood both structurally and functionally. The chaperone model for sHsp function provides a basic framework to explain the many proposed sHsp/protein interactions and potential functions. The diversity of the sHsp family, however, indicates that care must be taken in generalizing biochemical properties and activities across different family members. Nonetheless, the chapter has a firmer structural foundation on which to design future experiments to build a biochemical mechanism of action.
Databáze: OpenAIRE