Related Experiment Video
Updated: Sep 28, 2025

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
Published on: August 28, 2012
The Relationship between APOL1 Structure and Function: Clinical Implications
Sethu M Madhavan1, Matthias Buck2
1Department of Medicine, The Ohio State University, Columbus, Ohio.
Abstract:
Common variants in the APOL1 gene are associated with an increased risk of nondiabetic kidney disease in individuals of African ancestry. Mechanisms by which APOL1 variants mediate kidney disease pathogenesis are not well understood. Amino acid changes resulting from the kidney disease-associated APOL1 variants alter the three-dimensional structure and conformational dynamics of the C-terminal α-helical domain of the protein, which can rationalize the functional consequences. Understanding the three-dimensional structure of the protein, with and without the risk variants, can provide insights into the pathogenesis of kidney diseases mediated by APOL1 variants.
Related Concept Videos
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Protein Folding
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme...
Structural Protein Function
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
Cytoskeletal Linker Proteins - Plakins
Lysosomal Hydrolases

