Temperature-Induced Conformational Transition of Intestinal Fatty Acid Binding Protein Enhancing Ligand Binding:  A Functional, Spectroscopic, and Molecular Modeling Study†

Biochemistry ◽  
1998 ◽  
Vol 37 (47) ◽  
pp. 16802-16814 ◽  
Author(s):  
Cecilia N. Arighi ◽  
Juan Pablo F. C. Rossi ◽  
José M. Delfino
Keyword(s):  
Fatty Acid ◽  
Molecular Modeling ◽  
Ligand Binding ◽  
Fatty Acid Binding Protein ◽  
Conformational Transition ◽  
Binding Protein ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Molecular Modeling Study ◽  
Modeling Study

scholarly journals Effect on ligand binding of arginine mutations in recombinant rat liver fatty acid-binding protein

1994 ◽  
Vol 297 (1) ◽  
pp. 103-107 ◽  
Author(s):  
A E Thumser ◽  
C Evans ◽  
A F Worrall ◽  
D C Wilton
Keyword(s):  
Fatty Acid ◽  
Ligand Binding ◽  
Rat Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Wide Range ◽  
Arginine Residues

Rat liver fatty acid-binding protein is able to accommodate a wide range of non-polar anions in addition to long-chain fatty acids. The two arginine residues of rat liver fatty acid-binding protein, Arg122 and Arg126, have been mutated and the effect of mutation on ligand binding investigated. No significant decrease in affinity for the fluorescent fatty acid analogue, 11-(5-dimethylaminonaphthalenesulphonyl amino)undecanoic acid, or oleate was observed. However, the apparent affinity for oleoyl-CoA was slightly increased with the mutations Ala122 and Gln122 such that oleoyl-CoA rather than oleate became the preferred ligand for these mutants. Small changes in protein stability were observed with the Arg122 mutations. The lack of notable ionic involvement of the conserved internal residue Arg122 in ligand binding is consistent with the hypothesis that the mode of ligand binding in liver fatty acid-binding protein is markedly different from that of other members of this lipid-binding protein family.

Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein

2013 ◽  
Vol 48 (8) ◽  
pp. i-i
Author(s):  
C. Santambrogio ◽  
F. Favretto ◽  
M. D'Onofrio ◽  
M. Assfalg ◽  
R. Grandori ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Fatty Acid ◽  
Ligand Binding ◽  
Human Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Nmr Analysis ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

Ligand Binding Promiscuity of Human Liver Fatty Acid Binding Protein: Structural and Dynamic Insights from an Interaction Study with Glycocholate and Oleate

ChemBioChem ◽  
2013 ◽  
Vol 14 (14) ◽  
pp. 1807-1819 ◽  
Author(s):  
Filippo Favretto ◽  
Michael Assfalg ◽  
Mariana Gallo ◽  
Daniel Oscar Cicero ◽  
Mariapina D'Onofrio ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Ligand Binding ◽  
Human Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Interaction Study ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein

2013 ◽  
Vol 48 (8) ◽  
pp. 895-903 ◽  
Author(s):  
C. Santambrogio ◽  
F. Favretto ◽  
M. D'Onofrio ◽  
M. Assfalg ◽  
R. Grandori ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Fatty Acid ◽  
Ligand Binding ◽  
Human Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Nmr Analysis ◽  
Fatty Acid Binding ◽  
Acid Binding Protein
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