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

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.

Abstract

The recently revealed homology of the primary structures of ß-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 ß-lactoglobulin, retinol-binding protein and bilin-binding protein must be particularly suitable for binding of various hydrophobic ligands of small molecular mass.