TY - JOUR
T1 - The low-density lipoprotein receptor
T2 - Ligands, debates and lore
AU - Rudenko, Gabby
AU - Deisenhofer, Johann
PY - 2003/12
Y1 - 2003/12
N2 - Like pieces belonging to a large mosaic, the structures of low-density lipoprotein receptor (LDL-R) modules have been elucidated one by one in recent years. LDL-Rs localized on hepatocytes play an important role in removing cholesterol-transporting LDL particles from the plasma by receptor-mediated endocytosis. Key steps in this process involve the LDL-R binding LDL at neutral pH at the cell surface and, after internalization, releasing it again at acidic pH in the endosomes. How the modules of the LDL-R might interact within the intact receptor to carry out ligand binding and release has been revealed by the recent crystal structure of the extracellular domain of the LDL-R.
AB - Like pieces belonging to a large mosaic, the structures of low-density lipoprotein receptor (LDL-R) modules have been elucidated one by one in recent years. LDL-Rs localized on hepatocytes play an important role in removing cholesterol-transporting LDL particles from the plasma by receptor-mediated endocytosis. Key steps in this process involve the LDL-R binding LDL at neutral pH at the cell surface and, after internalization, releasing it again at acidic pH in the endosomes. How the modules of the LDL-R might interact within the intact receptor to carry out ligand binding and release has been revealed by the recent crystal structure of the extracellular domain of the LDL-R.
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U2 - 10.1016/j.sbi.2003.10.001
DO - 10.1016/j.sbi.2003.10.001
M3 - Review article
C2 - 14675545
AN - SCOPUS:0346850975
SN - 0959-440X
VL - 13
SP - 683
EP - 689
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 6
ER -