Two structural and functional domains of MESD required for proper folding and trafficking of LRP5/6.

@article{Chen2011TwoSA,
  title={Two structural and functional domains of MESD required for proper folding and trafficking of LRP5/6.},
  author={Jianglei Chen and Chia-Chen Liu and Qianqian Li and Christian Nowak and Guojun Bu and Jianjun Wang},
  journal={Structure},
  year={2011},
  volume={19 3},
  pages={313-23}
}
How the endoplasmic reticulum (ER) folding machinery coordinates general and specialized chaperones during protein translation and folding remains an important unanswered question. Here, we show two structural domains in MESD, a specialized chaperone for LRP5/6, carry out dual functions. The chaperone domain forms a complex with the immature receptor, maintaining the β-propeller (BP) domain in an interaction competent state for epidermal growth factor-repeat binding. This promotes proper… CONTINUE READING
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