Structure of the LDL Receptor Extracellular Domain at Endosomal pH

@article{Rudenko2002StructureOT,
  title={Structure of the LDL Receptor Extracellular Domain at Endosomal pH},
  author={Gabby Rudenko and Lisa Henry and Keith Henderson and Konstantin Ichtchenko and Michael S. Brown and Joseph L. Goldstein and Johann Deisenhofer},
  journal={Science},
  year={2002},
  volume={298},
  pages={2353 - 2358}
}
The low-density lipoprotein receptor mediates cholesterol homeostasis through endocytosis of lipoproteins. It discharges its ligand in the endosome at pH < 6. In the crystal structure at pH = 5.3, the ligand-binding domain (modules R2 to R7) folds back as an arc over the epidermal growth factor precursor homology domain (the modules A, B, β propeller, and C). The modules R4 and R5, which are critical for lipoprotein binding, associate with the β propeller via their calcium-binding loop. We… 
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