Isolation, amino acid sequence determination and binding properties of two fatty acid-binding proteins from axolotl (Ambistoma mexicanum) liver. Evolutionary relationships

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Amino acid sequence, binding properties, and evolutionary relationships of the basic liver fatty acid-binding protein from the catfish Rhamdia sapo

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Presence of intestinal, liver and heart/adipocyte fatty acid-binding protein types in the liver of a chimaera fish

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Presence of a fatty acid-binding protein in the armadillo Harderian gland

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Crystal structure of axolotl (Ambystoma mexicanum) liver bile acid-binding protein bound to cholic and oleic acid

The family of the liver bile acid-binding proteins (L-BABPs), formerly called liver basic fatty acid-binding proteins (Lb-FABPs) shares fold and sequence similarity with the paralogous liver fatty acid-binding proteins (L-FABPs) but has a different stoichiometry and specificity of ligand binding. This article describes the first X-ray structure of a member of the L-BABP family, axolotl (Ambystoma mexicanum) L-BABP, bound to two different ligands: cholic and oleic acid. The protein binds one molecule of oleic acid in a position that is significantly different from that of either of the two molecules that bind to rat liver FABP. The stoichiometry of binding of cholate is of two ligands per protein molecule, as observed in chicken L-BABP. The cholate molecule that binds buried most deeply into the internal cavity overlaps well with the analogous bound to chicken L-BABP, whereas the second molecule, which interacts with the first only through hydrophobic contacts, is more external and exposed to the solvent