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3CY4

Crystal Structure cation-dependent mannose 6-phosphate receptor at pH 7.4

Replaces:  2RL6
Summary for 3CY4
Entry DOI10.2210/pdb3cy4/pdb
Related2RL7 2RL8 2RL9 2RLB
DescriptorCation-dependent mannose-6-phosphate receptor, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCEROL, ... (4 entities in total)
Functional Keywordsp-type lectin, receptor, mannose 6-phosphate, lectin, glycoprotein, lysosome, membrane, transmembrane, transport, protein transport, sugar binding protein
Biological sourceBos taurus (cattle)
Cellular locationLysosome membrane ; Single-pass type I membrane protein : P11456
Total number of polymer chains2
Total formula weight36800.90
Authors
Olson, L.J.,Hindsgaul, O.,Dahms, N.M.,Kim, J.-J.P. (deposition date: 2008-04-25, release date: 2008-05-13, Last modification date: 2024-12-25)
Primary citationOlson, L.J.,Hindsgaul, O.,Dahms, N.M.,Kim, J.J.
Structural Insights into the Mechanism of pH-dependent Ligand Binding and Release by the Cation-dependent Mannose 6-Phosphate Receptor.
J.Biol.Chem., 283:10124-10134, 2008
Cited by
PubMed Abstract: The cation-dependent mannose 6-phosphate receptor (CD-MPR) is a key component of the lysosomal enzyme targeting system that binds newly synthesized mannose 6-phosphate (Man-6-P)-containing acid hydrolases and transports them to endosomal compartments. The interaction between the MPRs and its ligands is pH-dependent; the homodimeric CD-MPR binds lysosomal enzymes optimally in the pH environment of the trans Golgi network (pH approximately 6.5) and releases its cargo in acidic endosomal compartments (PubMed: 18272523
DOI: 10.1074/jbc.M708994200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.51 Å)
Structure validation

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