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Receptor-mediated Endocytosis

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Structure of Lipids

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Lipids include a diverse group of compounds that are largely nonpolar in nature. This is because they are hydrocarbons that include mostly nonpolar carbon-carbon or carbon-hydrogen bonds. Non-polar molecules are hydrophobic (“water fearing”), or insoluble in water. Lipids perform many different functions in a cell. Cells store energy for long-term use in the form of fats. Lipids also provide insulation from the environment for plants and animals. For example, they help keep aquatic birds and...

Structure of Lipids

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Lipids include a diverse group of compounds that are largely nonpolar in nature. This is because they are hydrocarbons that include mostly nonpolar carbon-carbon or carbon-hydrogen bonds. Non-polar molecules are hydrophobic (“water fearing”), or insoluble in water. Lipids perform many different functions in a cell. Cells store energy for long-term use in the form of fats. Lipids also provide insulation from the environment for plants and animals. For example, they help keep aquatic birds and...

Receptor-mediated Endocytosis

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Structure of Lipids

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Lipids include a diverse group of compounds that are largely nonpolar in nature. This is because they are hydrocarbons that include mostly nonpolar carbon-carbon or carbon-hydrogen bonds. Non-polar molecules are hydrophobic (“water fearing”), or insoluble in water. Lipids perform many different functions in a cell. Cells store energy for long-term use in the form of fats. Lipids also provide insulation from the environment for plants and animals. For example, they help keep aquatic birds and...

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Related Experiment Video

Updated: Jul 11, 2026

Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy

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Low-density lipoprotein receptor structure and folding.

J Gent¹, I Braakman

¹Department of Bio-organic Chemistry 1, Utrecht University, Padualaan 8, 3584, CH Utrecht, The Netherlands.

Cellular and Molecular Life Sciences : CMLS

|November 5, 2004

Summary

The endoplasmic reticulum (ER) quality control ensures proper protein folding. Misfolded low-density lipoprotein receptors (LDLR) in familial hypercholesterolemia impair cholesterol clearance, increasing cardiac disease risk.

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Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy

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Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

The endoplasmic reticulum (ER) is a critical cellular organelle for protein synthesis and folding.
Protein misfolding within the ER can lead to various diseases.
The low-density lipoprotein receptor (LDLR) is essential for cholesterol metabolism.

Purpose of the Study:

To review the structural characteristics of the LDLR.
To examine the folding pathway of the LDLR within the ER.
To compare the LDLR with other members of its structural family.

Main Methods:

Literature review of structural biology studies.
Analysis of protein folding mechanisms in the ER.
Comparative analysis of LDLR family members.

Main Results:

The LDLR undergoes a complex folding process in the ER, subject to quality control mechanisms.
Mutations in LDLR cause protein misfolding, leading to familial hypercholesterolemia.
Impaired LDLR function results in reduced LDL clearance and elevated blood cholesterol.

Conclusions:

Understanding LDLR structure and folding is crucial for addressing familial hypercholesterolemia.
ER protein quality control plays a vital role in preventing diseases associated with protein misfolding.
Further research into LDLR family members may reveal new therapeutic targets.