The complex interplay between ligand binding and conformational structure of the folate binding protein (folate receptor): Biological perspectives.

摘要: This review analyzes how interplay between folate binding and changes in protein (FBP) conformation/self-association affects the biological function of FBP. Concentration-dependent, reversible self-association hydrophobic apo-FBP at pI=7.4 is associated with decreased affinity for folate, probably due to shielding sites interacting patches. Titration removes apo-monomers, favoring dissociation self-associated into apo-monomers. Folate anchors FBP through a network hydrogen bonds interactions, induces conformational change formation hydrophilic stable holo-FBP. Holo-FBP exhibits ligand-mediated concentration-dependent multimers great thermal chemical stability strong intermolecular forces. Both ligand are thus protected against biological/physicochemical decomposition. In fluids low concentrations, e.g., saliva, semen plasma, apo-monomers holo-monomers associate asymmetrical complexes aberrant kinetics unless detergents, cholesterol or phospholipids present.