Solution structure of fatty acid-binding protein from human brain

2002 ◽  
pp. 61-68
Author(s):  
Martin Rademacher ◽  
Aukje W. Zimmerman ◽  
Heinz Rüterjans ◽  
Jacques H. Veerkamp ◽  
Christian Lücke
Keyword(s):  
Fatty Acid ◽  
Human Brain ◽  
Solution Structure ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

Solution structure of bovine heart fatty acid-binding protein (H-FABPC)

1993 ◽  
pp. 15-22
Author(s):  
Dirck Lassen ◽  
Christian Lücke ◽  
Arno Kromminga ◽  
Axel Lezius ◽  
Friedrich Spener ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Solution Structure ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Bovine Heart

Isolation and expression of a cDNA for human brain fatty acid-binding protein (B-FABP)

1997 ◽  
Vol 1354 (1) ◽  
pp. 24-28 ◽  
Author(s):  
Fumio Shimizu ◽  
Takeshi K Watanabe ◽  
Hiroichi Shinomiya ◽  
Yusuke Nakamura ◽  
Tsutomu Fujiwara
Keyword(s):  
Fatty Acid ◽  
Human Brain ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Protein B

Fatty Acid–Binding Protein 5 Mediates the Uptake of Fatty Acids, but not Drugs, Into Human Brain Endothelial Cells

2018 ◽  
Vol 107 (4) ◽  
pp. 1185-1193 ◽  
Author(s):  
Gordon S. Lee ◽  
Yijun Pan ◽  
Martin J. Scanlon ◽  
Christopher J.H. Porter ◽  
Joseph A. Nicolazzo
Keyword(s):  
Fatty Acids ◽  
Endothelial Cells ◽  
Fatty Acid ◽  
Human Brain ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Brain Endothelial Cells ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

scholarly journals Crystal Structure and Thermodynamic Analysis of Human Brain Fatty Acid-binding Protein

2000 ◽  
Vol 275 (35) ◽  
pp. 27045-27054
Author(s):  
Ganesaratnam K. Balendiran ◽  
Frank Schnütgen ◽  
Giovanna Scapin ◽  
Torsten Börchers ◽  
Ning Xhong ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Fatty Acid ◽  
Human Brain ◽  
Thermodynamic Analysis ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

Solution structure of bovine heart fatty acid-binding protein (H-FABPc)

1993 ◽  
Vol 123 (1-2) ◽  
pp. 15-22 ◽  
Author(s):  
Dirck Lassen ◽  
Christian L�cke ◽  
Arno Kromminga ◽  
Axel Lezius ◽  
Friedrich Spener ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Solution Structure ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Bovine Heart

scholarly journals Solution Structure and Backbone Dynamics of Human Liver Fatty Acid Binding Protein: Fatty Acid Binding Revisited

2012 ◽  
Vol 102 (11) ◽  
pp. 2585-2594 ◽  
Author(s):  
Jun Cai ◽  
Christian Lücke ◽  
Zhongjing Chen ◽  
Ye Qiao ◽  
Elena Klimtchuk ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Human Liver ◽  
Solution Structure ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Backbone Dynamics ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

Crystal structure of human brain-type fatty acid-binding protein FABP7 complexed with palmitic acid

2021 ◽  
Vol 77 (7) ◽  
Author(s):  
Ki Hyun Nam
Keyword(s):  
Crystal Structure ◽  
Fatty Acids ◽  
Fatty Acid ◽  
Human Brain ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Binding Pocket ◽  
Aliphatic Chain ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

The brain-type fatty acid-binding protein FABP7, which is expressed in astrocytes and neural progenitors, is a member of the intracellular lipid-binding protein family. This protein is not only involved in various cellular functions such as metabolism, inflammation and energy homeostasis, but also in diseases such as cognitive disorders and tumors. Structures of unsaturated fatty acids, such as oleic acid (OA) and docosahexaenoic acid (DHA), bound to FABP7 have been elucidated; however, structures of saturated fatty acids bound to FABP7 remain unknown. To better understand fatty acid recognition, here the crystal structure of human brain-type fatty acid-binding protein FABP7 complexed with palmitic acid (PA), a saturated fatty acid, is reported at a resolution of 1.6 Å. The PA bound to the fatty acid-binding pocket of FABP7 assumed a U-shaped conformation. The carboxylate moiety of PA interacted with Tyr129, Arg127 and, via a water bridge, with Arg107 and Thr54, whereas its aliphatic chain was stabilized by hydrophobic interactions with Met21, Leu24, Thr30, Thr37, Pro39, Phe58 and Asp77. Structural comparison showed that PA, OA and DHA exhibited unique binding conformations in the fatty acid-binding pocket, stabilized by distinct amino-acid interactions. The binding of PA to FABP7 exhibits a unique binding conformation when compared with other human FABPs (FABP3–FABP5 and FABP8) expressed in other tissues. Based on the crystal and fatty acid structures, it was suggested that PA, which prefers a linear form in nature, required a greater conformational change in its aliphatic chain to bind to the fatty acid-binding pocket in a U-shaped conformation, compared with the cis configurations of OA or DHA. This, together with the length of the aliphatic chain, was considered to be one of the factors determining the binding affinity of PA to FABP7. These results provide a better understanding of fatty acid recognition by FABP7 and expand the knowledge of the binding of PA to FABPs.

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