Journal Article10.1021/BI0489661
Crystal Structure of Chicken Liver Basic Fatty Acid-Binding Protein Complexed with Cholic Acid†,‡
Daniele Nichesola,Massimiliano Perduca,Stefano Capaldi,Maria E. Carrizo,Pier Giorgio Righetti,Hugo L. Monaco +5 more
TL;DR: The crystal structure of chicken Lb-FABP complexed with cholic acid and that of the apoprotein refined to 2.0 A resolution are presented and the possibility that the L-FabPs might be more appropriately called liver bile acid-binding proteins (L-BABPs) is suggested.
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Abstract: Two paralogous groups of liver fatty acid-binding proteins (FABPs) have been described: the mammalian type liver FABPs and the basic type (Lb-FABPs) characterized in several vertebrates but not in mammals. The two groups have similar sequences and share a highly conserved three-dimensional structure, but their specificity and stoichiometry of binding are different. The crystal structure of chicken Lb-FABP complexed with cholic acid and that of the apoprotein refined to 2.0 A resolution are presented in this paper. The two forms of the protein crystallize in different space groups, and significant changes are observed between the two conformations. The holoprotein binds two molecules of cholate in the interior cavity, and the contacts observed between the two ligands can help to explain the reason for this stoichiometry of binding. Most of the amino acids involved in ligand binding are conserved in other members of the Lb-FABP family. Since the amino acid sequence of the Lb-FABPs is more similar to that of the bile acid-binding proteins than to that of the L-FABPs, the possibility that the Lb-FABPs might be more appropriately called liver bile acid-binding proteins (L-BABPs) is suggested.
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Citations
Structural and dynamic roles of permanent water molecules in ligand molecular recognition by chicken liver bile acid binding protein.
Piero Ricchiuto,Alessandro Guerini Rocco,Elisabetta Gianazza,Dario Corrada,Tiziana Beringhelli,Ivano Eberini +5 more
TL;DR: Two 100 ns molecular dynamics simulations in explicit solvent for chicken liver bile acid binding protein, as apo form and as a complex with two molecules of cholic acid, and analyzed in detail the dynamics properties of all water molecules revealed a conserved pattern of hydrogen bonds between a single water molecule and three amino acid residues of the binding site.
Conformational plasticity of the lipid transfer protein SCP2.
Fabian V. Filipp,Michael Sattler +1 more
TL;DR: NMR relaxation measurements reveal that residues in the three C-terminal alpha-helices within the lipid binding region exhibit mobility at fast and slow time scales, and may play a role for the access of hydrophobic ligands to an occluded binding pocket.
Bile acid binding protein: a versatile host of small hydrophobic ligands for applications in the fields of MRI contrast agents and bio-nanomaterials.
Katiuscia Pagano,Simona Tomaselli,Serena Zanzoni,Michael Assfalg,Henriette Molinari,Laura Ragona +5 more
TL;DR: The beta-clamshell family of intracellular lipid binding proteins share a stable beta-barrel fold, delimiting an internal cavity capable of promiscuous ligand binding and display significant flexibility at the putative ligand portal, which make this class of proteins good scaffolds to build host-guest systems for applications in nanomedicine and nanomaterials.
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