The low-density lipoprotein receptor: ligands, debates and lore.
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.
Rudenko
Gabby
G
Department of Biochemistry, UT Southwestern Medical Center, 5323 Harry Hines Boulevard Y 4-206, Dallas, TX 75390-9050, USA.
Deisenhofer
Johann
J
D000818:Animals; D001665:Binding Sites; D001693:Biological Transport, Active / Q000502:physiology; D004705:Endocytosis / Q000502:physiology*; D011992:Endosomes / Q000378:metabolism; D004815:Epidermal Growth Factor / Q000737:chemistry* / Q000378:metabolism*; D022781:Hepatocytes / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D008077:Lipoproteins, LDL / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011973:Receptors, LDL / Q000737:chemistry* / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology; D013329:Structure-Activity Relationship
D008024:Ligands; D008077:Lipoproteins, LDL; D011973:Receptors, LDL; D004815:Epidermal Growth Factor