2RL8
Crystal Structure cation-dependent mannose 6-phosphate receptor at pH 6.5 bound to M6P
Summary for 2RL8
| Entry DOI | 10.2210/pdb2rl8/pdb |
| Related | 2RL6 2RL7 2RL9 2RLB |
| Descriptor | Cation-dependent mannose-6-phosphate receptor, 2-acetamido-2-deoxy-beta-D-glucopyranose, MANGANESE (II) ION, ... (5 entities in total) |
| Functional Keywords | p-type lectin, receptor, mannose 6-phosphate, lectin, glycoprotein, lysosome, membrane, transmembrane, transport, protein transport, sugar binding protein |
| 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 | 35959.72 |
| Authors | Olson, L.J.,Hindsgaul, O.,Kim, J.-J.P.,Dahms, N.M. (deposition date: 2007-10-18, release date: 2008-02-12, Last modification date: 2024-11-13) |
| Primary citation | Olson, 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 ( DOI: 10.1074/jbc.M708994200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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