Molecular studies of pH-dependent ligand interactions with the low-density lipoprotein receptor

A site-directed mutagenesis studies were carried out to understand the role of histidines His190, His562, and His586 in recombinant soluble low-density lipoprotein receptor (sLDLR) in pH-dependent ligand binding and discharge. The data obtained confirmed the existence of a cryptic, histidine side chain ionization-dependent alternative ligand that regulates ligand discharge via conformational reorganization.