1Q25

Crystal structure of N-terminal 3 domains of CI-MPR

Summary for 1Q25

• Entry DOI: 10.2210/pdb1q25/pdb
• Related: 1SYO 1SZ0
• Descriptor: cation-independent mannose 6-phosphate receptor, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: p-lectin, receptor, mannose 6-phosphate, protein transport, sugar binding protein
• Biological source: Bos taurus (cattle)
• Total number of polymer chains: 1
• Total formula weight: 49045.78

Authors

Olson, L.J.,Dahms, N.M.,Kim, J.-J.P. (deposition date: 2003-07-23, release date: 2004-06-29, Last modification date: 2020-07-29)

Primary citation

Olson, L.J.,Yammani, R.D.,Dahms, N.M.,Kim, J.-J.P.
Structure of uPAR, plasminogen, and sugar-binding sites of the 300 kDa mannose 6-phosphate receptor
Embo J., 23:2019-2028, 2004

PubMed Abstract: The 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR) mediates the intracellular transport of newly synthesized lysosomal enzymes containing mannose 6-phosphate on their N-linked oligosaccharides. In addition to its role in lysosome biogenesis, the CI-MPR interacts with a number of different extracellular ligands at the cell surface, including latent transforming growth factor-beta, insulin-like growth factor-II, plasminogen, and urokinase-type plasminogen activator receptor (uPAR), to regulate cell growth and motility. We have solved the crystal structure of the N-terminal 432 residues of the CI-MPR at 1.8 A resolution, which encompass three out of the 15 repetitive domains of its extracytoplasmic region. The three domains, which exhibit similar topology to each other and to the 46 kDa cation-dependent mannose 6-phosphate receptor, assemble into a compact structure with the uPAR/plasminogen and the carbohydrate-binding sites situated on opposite faces of the molecule. Knowledge of the arrangement of these three domains has allowed us to propose a model of the entire extracytoplasmic region of the CI-MPR that provides a context with which to envision the numerous binding interactions carried out by this multi-faceted receptor.

PubMed: 15085180
DOI: 10.1038/sj.emboj.7600215

Experimental method

X-RAY DIFFRACTION (1.8 Å)