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Updated: Jul 7, 2026

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
Published on: August 26, 2025
Structural insights into the mechanism of pH-dependent ligand binding and release by the cation-dependent mannose
Linda J Olson1, Ole Hindsgaul, Nancy M Dahms
1Department of Biochemistry, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI 53226, USA.
Abstract:
The cation-dependent mannose 6-phosphate receptor (CD-MPR) is a key component of the lysosomal enzyme targeting system that binds newly synthesized mannose 6-phosphate (Man-6-P)-containing acid hydrolases and transports them to endosomal compartments. The interaction between the MPRs and its ligands is pH-dependent; the homodimeric CD-MPR binds lysosomal enzymes optimally in the pH environment of the trans Golgi network (pH approximately 6.5) and releases its cargo in acidic endosomal compartments (
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