NDLI: Low-density lipoprotein receptor structure and folding

Content Provider	Springer Nature Link
Author	Gent, J. Braakman, I.
Copyright Year	2004
Abstract	The endoplasmic reticulum (ER) is a major cellular ‘production factory’ for many membrane and soluble proteins. A quality control system ensures that only correctly folded and assembled proteins leave the compartment. The low-density lipoprotein receptor (LDLR) is the prototype of a large family of structurally homologous cell surface receptors, which fold in the ER and function as endocytic and signaling receptors in a wide variety of cellular processes. Patients with familial hypercholesterolemia carry single or multiple mutations in their LDLR, which leads to malfunction of the protein, in most patients through misfolding of the receptor. As a result, clearance of cholesterol-rich LDL particles from the circulation decreases, and the elevated blood cholesterol levels cause early onset of atherosclerosis and an increased risk of cardiac disease in these patients. In this review, we will elaborate on the structural aspects of the LDLR and its folding pathway and compare it to other LDLR family members.
Starting Page	2461
Ending Page	2470
Page Count	10
File Format	PDF
ISSN	1420682X
Journal	Cellular and Molecular Life Sciences
Volume Number	61
Issue Number	19
e-ISSN	14209071
Language	English
Publisher	Birkhäuser-Verlag
Publisher Date	2004-01-01
Publisher Place	Basel
Access Restriction	Subscribed
Subject Keyword	LDL receptor structure folding chaperones disulfide bonds Biomedicine general Life Sciences Biochemistry Cell Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology Molecular Medicine Pharmacology Cellular and Molecular Neuroscience

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