Article
Two structural and functional domains of MESD required for proper folding and trafficking of LRP5/6.
Structure (London, England : 1993) - 9 Mar 2011
Chen Jianglei, Liu Chia-Chen, Li Qianqian, Nowak Christian, Bu Guojun, Wang Jianjun
Abstract excerpt
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...
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