| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2047461 | FEBS Letters | 2015 | 6 Pages |
•The effects of the FABP3 Asp3Gly polymorphism on protein structure and function were investigated.•The Asp3Gly mutation decreases FABP3 intracellular stability.•The Asp3Gly mutation also influences FABP3 subcellular localization.
Fatty acid-binding proteins (FABP) play a crucial role in intracellular fatty acid transportation and metabolism. In this study, we investigate the effects of the FABP3 Asp3Gly (D3G) polymorphism on protein structure and function. Although the mutation did not alter protein secondary structure or the ability to bind 1-anilinonaphthalene-8-sulfonic acid and palmitate, the intracellular stability of the D3G mutant was significantly decreased. Immunocytochemical analysis reveals that the mutation alters FABP3 subcellular localization. Our results suggest that the D3G polymorphism may impact energy metabolism and physiological functions.
