Identification of amino acid residues that determine pH dependence of ligand binding to the asialoglycoprotein receptor during endocytosis.

@article{Wragg1999IdentificationOA,
  title={Identification of amino acid residues that determine pH dependence of ligand binding to the asialoglycoprotein receptor during endocytosis.},
  author={St{\'e}phanie Wragg and Kurt Drickamer},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 50},
  pages={35400-6}
}
The rat hepatic asialoglycoprotein receptor mediates clearance of galactose- and N-acetylgalactosamine-terminated glycoproteins by endocytosis, binding ligands through a C-type, Ca(2+)-dependent carbohydrate-recognition domain (CRD) at extracellular pH and releasing them at lower pH in endosomes. At physiological Ca(2+) concentrations, the midpoint for ligand release from the CRD of the major subunit of the receptor is pH 7.1. In contrast, the midpoint is pH 5.0 for a galactose-binding… CONTINUE READING

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Introduction of histidine and aspartic acid residues into the mannose - binding protein CRD at positions equivalent to His(256 ) and Asp(266 ) raises the pH for half - maximal binding of ligand to 6.1 .
Introduction of histidine and aspartic acid residues into the mannose - binding protein CRD at positions equivalent to His(256 ) and Asp(266 ) raises the pH for half - maximal binding of ligand to 6.1 .
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