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J. Biol. Chem., Vol. 263, Issue 20, 9752-9760, Jul, 1988

Conformational changes in the chicken receptor for endocytosis of glycoproteins. Modulation of ligand-binding activity by Ca2+ and pH

JA Loeb and K Drickamer
Department of Biochemistry and Molecular Biology, University of Chicago, Illinois 60637.

Limited proteolysis, gel filtration, and circular dichroism have been used to identify at least three distinct conformational states of a proteolytic fragment containing the ligand-binding domain of the chicken receptor for endocytosis of glycoproteins. Differences in the ligand-binding activity of intact receptor brought about by changing Ca2+ concentrations and pH values can be correlated with different physical states of the binding domain present under similar conditions. An active, ligand-binding state can be detected at either pH 7.8 or 5.4, but 10-fold higher concentrations of Ca2+ are required to stabilize this state at the lower pH. In all cases, the dependence on Ca2+ concentration is second-order, suggesting that two Ca2+ ions are bound to each domain. These studies demonstrate an interdependence between the effects of Ca2+ concentration and pH on both ligand-binding activity and receptor conformation, which is important to consider when describing the binding and dissociation of ligand during endocytosis.
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