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1q25
From Proteopedia
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| - | [[Image:1q25.gif|left|200px]] | + | [[Image:1q25.gif|left|200px]] |
| - | + | ||
| - | '''Crystal structure of N-terminal 3 domains of CI-MPR''' | + | {{Structure |
| + | |PDB= 1q25 |SIZE=350|CAPTION= <scene name='initialview01'>1q25</scene>, resolution 1.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= IGF2R ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of N-terminal 3 domains of CI-MPR''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1Q25 is a [ | + | 1Q25 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q25 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15085180 15085180] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: receptor]] | [[Category: receptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:32:05 2008'' |
Revision as of 11:32, 20 March 2008
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| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | IGF2R (Bos taurus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Thu Mar 20 13:32:05 2008
