1q25

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[[Image:1q25.gif|left|200px]]
[[Image:1q25.gif|left|200px]]
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{{Structure
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|PDB= 1q25 |SIZE=350|CAPTION= <scene name='initialview01'>1q25</scene>, resolution 1.80&Aring;
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The line below this paragraph, containing "STRUCTURE_1q25", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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|GENE= IGF2R ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus])
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|DOMAIN=
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{{STRUCTURE_1q25| PDB=1q25 | SCENE= }}
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|RELATEDENTRY=[[1syo|1SYO]], [[1sz0|1SZ0]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q25 OCA], [http://www.ebi.ac.uk/pdbsum/1q25 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q25 RCSB]</span>
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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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[[Category: Kim, J J.P.]]
[[Category: Kim, J J.P.]]
[[Category: Olson, L J.]]
[[Category: Olson, L J.]]
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[[Category: mannose 6-phosphate]]
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[[Category: Mannose 6-phosphate]]
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[[Category: p-lectin]]
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[[Category: P-lectin]]
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[[Category: receptor]]
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[[Category: Receptor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:46:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:07:47 2008''
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Revision as of 02:46, 3 May 2008

Image:1q25.gif

Template:STRUCTURE 1q25

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 Sat May 3 05:46:29 2008

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