Molecular basis of lysosomal enzyme recognition: Three-dimensional structure of the cation-dependent mannose 6-phosphate receptor

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Abstract

Targeting of newly synthesized lysosomal hydrolases to the lysosome is mediated by the cation-dependent mannose 6-phosphate receptor (CD-MPR) and the insulin-like growth factor II/cation-independent mannose 6-phosphate receptor (IGF-II/CI-MPR). The two receptors, which share sequence similarities, constitute the P-type family of animal lectins. We now report the three-dimensional structure of a glycosylation-deficient, yet fully functional form of the extracytoplasmic domain of the bovine CD-MPR (residues 3-154) complexed with mannose 6-phosphate at 1.8 Å resolution. The extracytoplasmic domain of the CD-MPR crystallizes as a dimer, and each monomer folds into a nine-stranded flattened β barrel, which bears a striking resemblance to avidin. The distance of 40 Å between the two ligand- binding sites of the dimer provides a structural basis for the observed differences in binding affinity exhibited by the CD-MPR toward various lysosomal enzymes.

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Roberts, D. L., Weix, D. J., Dahms, N. M., & Kim, J. J. P. (1998). Molecular basis of lysosomal enzyme recognition: Three-dimensional structure of the cation-dependent mannose 6-phosphate receptor. Cell, 93(4), 639–648. https://doi.org/10.1016/S0092-8674(00)81192-7

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