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The low-density lipoprotein receptor: ligands, debates and lore
Gabby Rudenko1, Johann Deisenhofer
1Department of Biochemistry, UT Southwestern Medical Center, 5323 Harry Hines Boulevard Y 4-206, Dallas, TX 75390-9050, USA.
Current Opinion in Structural Biology
|December 17, 2003
Summary
The low-density lipoprotein receptor (LDL-R) binds and releases LDL particles for cholesterol removal. Recent crystal structures reveal how LDL-R modules interact to perform these functions.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Low-density lipoprotein receptors (LDL-Rs) on hepatocytes are crucial for clearing plasma LDL cholesterol via receptor-mediated endocytosis.
- LDL-R function involves binding LDL at neutral pH on the cell surface and releasing it at acidic pH within endosomes.
Purpose of the Study:
- To elucidate the structural basis of LDL-R function in ligand binding and release.
- To understand how LDL-R modules interact within the intact receptor.
Main Methods:
- X-ray crystallography of the LDL-R extracellular domain.
Main Results:
- Individual LDL-R module structures have been determined.
- The recent crystal structure of the extracellular domain provides insights into module interactions.
- This structure reveals how LDL-R performs ligand binding and release.
Conclusions:
- The structural elucidation of LDL-R modules and their interactions is key to understanding cholesterol homeostasis.
- The crystal structure of the LDL-R extracellular domain offers a mechanistic view of LDL binding and release.