1m6p
From Proteopedia
|
EXTRACYTOPLASMIC DOMAIN OF BOVINE CATION-DEPENDENT MANNOSE 6-PHOSPHATE RECEPTOR
Overview
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.
About this Structure
1M6P is a Single protein structure of sequence from Bos taurus with MN and M6P as ligands. Full crystallographic information is available from OCA.
Reference
Molecular basis of lysosomal enzyme recognition: three-dimensional structure of the cation-dependent mannose 6-phosphate receptor., Roberts DL, Weix DJ, Dahms NM, Kim JJ, Cell. 1998 May 15;93(4):639-48. PMID:9604938
Page seeded by OCA on Tue Nov 20 21:11:18 2007
