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2RL9

Crystal Structure cation-dependent mannose 6-phosphate receptor at pH 6.5 bound to trimannoside

Summary for 2RL9
Entry DOI10.2210/pdb2rl9/pdb
Related2RL6 2RL7 2RL8 2RLB
DescriptorCation-dependent mannose-6-phosphate receptor, 6-O-phosphono-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 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 weight36608.29
Authors
Olson, L.J.,Hindsgaul, O.,Dahms, N.M.,Kim, J.-J.P. (deposition date: 2007-10-18, release date: 2008-02-12, Last modification date: 2024-10-09)
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 (2.4 Å)
Structure validation

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