1M6P

EXTRACYTOPLASMIC DOMAIN OF BOVINE CATION-DEPENDENT MANNOSE 6-PHOSPHATE RECEPTOR

Summary for 1M6P

• Entry DOI: 10.2210/pdb1m6p/pdb
• Descriptor: CATION-DEPENDENT MANNOSE-6-PHOSPHATE RECEPTOR, MANGANESE (II) ION, 6-O-phosphono-alpha-D-mannopyranose, ... (4 entities in total)
• Functional Keywords: receptor, cation dependent mannose 6-phosphate, p-type lectin, transport
• Biological source: Bos taurus (cattle)
• Cellular location: Lysosome membrane; Single-pass type I membrane protein: P11456
• Total number of polymer chains: 2
• Total formula weight: 35056.87

Authors

Roberts, D.L.,Weix, D.J.,Dahms, N.M.,Kim, J.J.-P. (deposition date: 1998-04-19, release date: 1999-04-27, Last modification date: 2024-10-30)

Primary citation

Roberts, D.L.,Weix, D.J.,Dahms, N.M.,Kim, J.J.
Molecular basis of lysosomal enzyme recognition: three-dimensional structure of the cation-dependent mannose 6-phosphate receptor.
Cell(Cambridge,Mass.), 93:639-648, 1998

PubMed 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 A resolution. The extracytoplasmic domain of the CD-MPR crystallizes as a dimer, and each monomer folds into a nine-stranded flattened beta barrel, which bears a striking resemblance to avidin. The distance of 40 A 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.

PubMed: 9604938
DOI: 10.1016/S0092-8674(00)81192-7

Experimental method

X-RAY DIFFRACTION (1.8 Å)