12 research outputs found
Crystal structure of chicken liver basic fatty acid-binding protein complexed with cholic acid
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 \uc5 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
Crystal Structure of Chicken Liver Basic Fatty Acid-Binding Protein complexed with cholic acid
Crystal Structure of Chicken Liver Basic Fatty Acid-Binding Protein complexed with cholic aci