Wrapping the alpha-crystallin domain fold in a chaperone assembly.

@article{Stamler2005WrappingTA,
  title={Wrapping the alpha-crystallin domain fold in a chaperone assembly.},
  author={Robin Stamler and Guido Kapp{\'e} and Wilbert C. Boelens and Christine Slingsby},
  journal={Journal of molecular biology},
  year={2005},
  volume={353 1},
  pages={68-79}
}
Small heat shock proteins (sHsps) are oligomers that perform a protective function by binding denatured proteins. Although ubiquitous, they are of variable sequence except for a C-terminal approximately 90-residue "alpha-crystallin domain". Unlike larger stress response chaperones, sHsps are ATP-independent and generally form polydisperse assemblies. One proposed mechanism of action involves these assemblies breaking into smaller subunits in response to stress, before binding unfolding… CONTINUE READING
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