scholarly journals Crystal Structure of the Mp1p Ligand Binding Domain 2 Reveals Its Function as a Fatty Acid-binding Protein

2010 ◽  
Vol 285 (12) ◽  
pp. 9211-9220 ◽  
Author(s):  
Shuang Liao ◽  
Edward T. K. Tung ◽  
Wei Zheng ◽  
Ken Chong ◽  
Yuanyuan Xu ◽  
...  
1994 ◽  
Vol 297 (1) ◽  
pp. 103-107 ◽  
Author(s):  
A E Thumser ◽  
C Evans ◽  
A F Worrall ◽  
D C Wilton

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.


Author(s):  
Emma Jakobsson ◽  
Gabriela Alvite ◽  
Terese Bergfors ◽  
Adriana Esteves ◽  
Gerard J. Kleywegt

2000 ◽  
Vol 275 (35) ◽  
pp. 27045-27054
Author(s):  
Ganesaratnam K. Balendiran ◽  
Frank Schnütgen ◽  
Giovanna Scapin ◽  
Torsten Börchers ◽  
Ning Xhong ◽  
...  

Biochemistry ◽  
2004 ◽  
Vol 43 (44) ◽  
pp. 14072-14079 ◽  
Author(s):  
Daniele Nichesola ◽  
Massimiliano Perduca ◽  
Stefano Capaldi ◽  
Maria E. Carrizo ◽  
Pier Giorgio Righetti ◽  
...  

1990 ◽  
Vol 98 (1-2) ◽  
Author(s):  
Giovanna Scapin ◽  
Paola Spadon ◽  
Mario Mammi ◽  
Giuseppe Zanotti ◽  
HugoL. Monaco

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