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Strategies for carbohydrate recognition by the mannose 6-phosphate receptors Dahms NM; Olson LJ; Kim JJGlycobiology 2008[Sep]; 18 (9): 664-78The two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues.|*Carbohydrate Metabolism/physiology[MESH]|Amino Acid Sequence[MESH]|Animals[MESH]|Binding Sites[MESH]|Crystallography, X-Ray[MESH]|Glycoproteins/chemistry/metabolism/physiology[MESH]|Humans[MESH]|Mannosephosphates/chemistry/metabolism[MESH]|Models, Biological[MESH]|Models, Molecular[MESH]|Molecular Sequence Data[MESH]|Oligosaccharides/metabolism[MESH]|Protein Binding[MESH]|Receptor, IGF Type 2/chemistry/*metabolism[MESH]|Sequence Homology, Amino Acid[MESH] |
