1TW4

Crystal Structure of Chicken Liver Basic Fatty Acid Binding Protein (Bile Acid Binding Protein) Complexed With Cholic Acid

Summary for 1TW4

• Entry DOI: 10.2210/pdb1tw4/pdb
• Related: 1TVQ
• Descriptor: Fatty acid-binding protein, CHOLIC ACID (3 entities in total)
• Functional Keywords: lb-fabp, fabp, babp, intracellular bile acid-binding protein, cholic acid, bile acid, lipid binding protein
• Biological source: Gallus gallus (chicken)
• Cellular location: Cytoplasm: P80226
• Total number of polymer chains: 2
• Total formula weight: 29834.64

Authors

Nichesola, D.,Perduca, M.,Capaldi, S.,Carrizo, M.E.,Righetti, P.G.,Monaco, H.L. (deposition date: 2004-06-30, release date: 2004-11-23, Last modification date: 2024-03-13)

Primary citation

Nichesola, D.,Perduca, M.,Capaldi, S.,Carrizo, M.E.,Righetti, P.G.,Monaco, H.L.
Crystal structure of chicken liver basic Fatty Acid-binding protein complexed with cholic acid
Biochemistry, 43:14072-14079, 2004

PubMed 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.

PubMed: 15518556
DOI: 10.1021/bi0489661

Experimental method

X-RAY DIFFRACTION (2 Å)