Title : Fatty acids bind tightly to the N-terminal domain of angiopoietin-like protein 4 and modulate its interaction with lipoprotein lipase.

Pub. Date : 2012 Aug 24

PMID : 22773878






5 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Fatty acids bind tightly to the N-terminal domain of angiopoietin-like protein 4 and modulate its interaction with lipoprotein lipase. Fatty Acids angiopoietin like 4 Homo sapiens
2 In this study, we demonstrate that fatty acids reduce the inactivation of LPL by Angptl4. Fatty Acids angiopoietin like 4 Homo sapiens
3 Surface plasmon resonance, isothermal titration calorimetry, fluorescence, and chromatography measurements revealed that fatty acids bind with high affinity to ccd-Angptl4. Fatty Acids angiopoietin like 4 Homo sapiens
4 On binding of fatty acids, ccd-Angptl4 underwent conformational changes resulting in a decreased helical content, weakened structural stability, dissociation of oligomers, and altered fluorescence properties of the Trp-38 residue that is located close to the putative LPL-binding region. Fatty Acids angiopoietin like 4 Homo sapiens
5 Based on these results, we propose that fatty acids play an important role in modulating the effects of Angptl4. Fatty Acids angiopoietin like 4 Homo sapiens