| Literature DB >> 26206228 |
Tatsuya Kusudo1, Yasuhiko Hashida2, Fujiko Ando3, Hiroshi Shimokata4, Hitoshi Yamashita5.
Abstract
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.Entities:
Keywords: Fatty acid binding protein; Polymorphism; Protein stability; Single-nucleotide polymorphism; Subcellular localizatoin
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Year: 2015 PMID: 26206228 DOI: 10.1016/j.febslet.2015.07.007
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124