Structural basis for the antifolding activity of a molecular chaperone

@inproceedings{Huang2016StructuralBF,
  title={Structural basis for the antifolding activity of a molecular chaperone},
  author={Chengdong Huang and Paolo Rossi and Tomohide Saio and Charalampos G. Kalodimos},
  booktitle={Nature},
  year={2016}
}
Molecular chaperones act on non-native proteins in the cell to prevent their aggregation, premature folding or misfolding. Different chaperones often exert distinct effects, such as acceleration or delay of folding, on client proteins via mechanisms that are poorly understood. Here we report the solution structure of SecB, a chaperone that exhibits strong antifolding activity, in complex with alkaline phosphatase and maltose-binding protein captured in their unfolded states. SecB uses long… CONTINUE READING
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