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J Biol Chem, Vol. 274, Issue 52, 36905-36911, December 24, 1999

Mutational Analysis of the Binding Site Residues of the Bovine Cation-dependent Mannose 6-Phosphate Receptor*

Linda J. Olson, Michael K. Hancock, David Dix, Jung-Ja P. Kim, and Nancy M. DahmsDagger

From the Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin 53226

Mannose 6-phosphate receptors (MPRs) deliver soluble acid hydrolases to the lysosome in higher eukaryotic cells. The two MPRs, the cation-dependent MPR (CD-MPR) and the insulin-like growth factor II/cation-independent MPR, carry out this process by binding with high affinity to mannose 6-phosphate residues found on the N-linked oligosaccharides of their ligands. To elucidate the key amino acids involved in conveying this carbohydrate specificity, site-directed mutagenesis studies were conducted on the extracytoplasmic domain of the bovine CD-MPR. Single amino acid substitutions of the residues that form the binding pocket were generated, and the mutant constructs were expressed in transiently transfected COS-1 cells. Following metabolic labeling, mutant CD-MPRs were tested for their ability to bind pentamannosyl phosphate-containing affinity columns. Of the eight amino acids mutated, four (Gln-66, Arg-111, Glu-133, and Tyr-143) were found to be essential for ligand binding. In addition, mutation of the single histidine residue, His-105, within the binding site diminished the binding of the receptor to ligand, but did not eliminate the ability of the CD-MPR to release ligand under acidic conditions.

* This work was supported by Grant DK42667 from the National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger This work was done during the tenure of an Established Investigatorship from the American Heart Association. To whom correspondence should be addressed: Dept. of Biochemistry, Medical College of Wisconsin, 8701 Watertown Plank Rd., Milwaukee, WI 53226. Tel.: 414-456-4698; Fax: 414-456-6510; E-mail: ndahms@mcw.edu.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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