1q25
From Proteopedia
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Crystal structure of N-terminal 3 domains of CI-MPR
Overview
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.
About this Structure
1Q25 is a Single protein structure of sequence from Bos taurus with GOL as ligand. Full crystallographic information is available from OCA.
Reference
Structure of uPAR, plasminogen, and sugar-binding sites of the 300 kDa mannose 6-phosphate receptor., Olson LJ, Yammani RD, Dahms NM, Kim JJ, EMBO J. 2004 May 19;23(10):2019-28. Epub 2004 Apr 15. PMID:15085180
Page seeded by OCA on Wed Nov 21 00:19:12 2007
