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| [[Image:1q25.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1q25| PDB=1q25 | SCENE= }} | | {{STRUCTURE_1q25| PDB=1q25 | SCENE= }} |
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| '''Crystal structure of N-terminal 3 domains of CI-MPR'''
| | ===Crystal structure of N-terminal 3 domains of CI-MPR=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_15085180}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15085180 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15085180}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: P-lectin]] | | [[Category: P-lectin]] |
| [[Category: Receptor]] | | [[Category: Receptor]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:46:29 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:29:41 2008'' |
