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1SZ0

N-terminal 3 domains of CI-MPR bound to mannose 6-phosphate

Summary for 1SZ0
Entry DOI10.2210/pdb1sz0/pdb
Related1Q25 1SYO
Descriptorcation-independent mannose 6-phosphate receptor, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
Functional Keywordslectin; receptor; mannose 6-phosphate, protein transport, sugar binding protein
Biological sourceBos taurus (cattle)
Total number of polymer chains2
Total formula weight97632.07
Authors
Olson, L.J.,Dahms, N.M.,Kim, J.-J.P. (deposition date: 2004-04-01, release date: 2004-06-29, Last modification date: 2020-07-29)
Primary citationOlson, L.J.,Dahms, N.M.,Kim, J.-J.P.
The N-terminal carbohydrate recognition site of the cation-independent mannose 6-phosphate receptor
J.Biol.Chem., 279:34000-34009, 2004
Cited by
PubMed Abstract: The 300-kDa cation-independent mannose 6-phosphate receptor (CI-MPR) plays a critical role in the trafficking of newly synthesized mannose 6-phosphate-containing acid hydrolases to the lysosome. The receptor contains two high affinity carbohydrate recognition sites within its 15-domain extracytoplasmic region, with essential residues for carbohydrate recognition located in domain 3 and domain 9. Previous studies have shown that these two sites are distinct with respect to carbohydrate specificity. In addition, expression of truncated forms of the CI-MPR demonstrated that domain 9 can be expressed as an isolated domain, retaining high affinity (Kd approximately 1 nm) carbohydrate binding, whereas expression of domain 3 alone resulted in a protein capable of only low affinity binding (Kd approximately 1 microm) toward a lysosomal enzyme. In the current report the crystal structure of the N-terminal 432 residues of the CI-MPR, encompassing domains 1-3, was solved in the presence of bound mannose 6-phosphate. The structure reveals the unique architecture of this carbohydrate binding pocket and provides insight into the ability of this site to recognize a variety of mannose-containing sugars.
PubMed: 15169779
DOI: 10.1074/jbc.M404588200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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