The structural motif of beta-lactoglobulin and retinol-binding protein: a basic framework for binding and transport of small hydrophobic molecules?

Abstract

Abstract The recently revealed homology of the primary structures of s-lactoglobulin, retinol-binding protein, apolipoprotein D, α-1-microglobulin and BG protein from olfactory epithelium, suggests the existence of a new protein superfamily of hydrophobic molecule transporters. The common protein fold of s-lactoglobulin, retinol-binding protein and bilin-binding protein must be particularly suitable for binding of various hydrophobic ligands of small molecular mass.