1sz0: Difference between revisions
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'''N-terminal 3 domains of CI-MPR bound to mannose 6-phosphate''' | {{Structure | ||
|PDB= 1sz0 |SIZE=350|CAPTION= <scene name='initialview01'>1sz0</scene>, resolution 2.10Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=OS:OSMIUM+ION'>OS</scene> and <scene name='pdbligand=M6P:ALPHA-D-MANNOSE-6-PHOSPHATE'>M6P</scene> | |||
|ACTIVITY= | |||
|GENE= IGF2R, M6P ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | |||
}} | |||
'''N-terminal 3 domains of CI-MPR bound to mannose 6-phosphate''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1SZ0 is a [ | 1SZ0 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=1SZ0 OCA]. | ||
==Reference== | ==Reference== | ||
The N-terminal carbohydrate recognition site of the cation-independent mannose 6-phosphate receptor., Olson LJ, Dahms NM, Kim JJ, J Biol Chem. 2004 Aug 6;279(32):34000-9. Epub 2004 May 28. PMID:[http:// | The N-terminal carbohydrate recognition site of the cation-independent mannose 6-phosphate receptor., Olson LJ, Dahms NM, Kim JJ, J Biol Chem. 2004 Aug 6;279(32):34000-9. Epub 2004 May 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15169779 15169779] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lectin; receptor; mannose 6-phosphate]] | [[Category: lectin; receptor; mannose 6-phosphate]] | ||
''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 14:11:27 2008'' | ||
Revision as of 12:11, 20 March 2008
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| 1sz0, resolution 2.10Å | |||||||||||||
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| Ligands: | NAG, OS and M6P | ||||||||||||
| Gene: | IGF2R, M6P (Bos taurus) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
N-terminal 3 domains of CI-MPR bound to mannose 6-phosphate
Overview
The 300-kDa cation-independent mannose 6-phosphate receptor (CI-MPR) plays a critical role in the trafficking of newly synthesized mannose 6-phosphate-containing acid hydrolases to the lysosome. The receptor contains two high affinity carbohydrate recognition sites within its 15-domain extracytoplasmic region, with essential residues for carbohydrate recognition located in domain 3 and domain 9. Previous studies have shown that these two sites are distinct with respect to carbohydrate specificity. In addition, expression of truncated forms of the CI-MPR demonstrated that domain 9 can be expressed as an isolated domain, retaining high affinity (Kd approximately 1 nm) carbohydrate binding, whereas expression of domain 3 alone resulted in a protein capable of only low affinity binding (Kd approximately 1 microm) toward a lysosomal enzyme. In the current report the crystal structure of the N-terminal 432 residues of the CI-MPR, encompassing domains 1-3, was solved in the presence of bound mannose 6-phosphate. The structure reveals the unique architecture of this carbohydrate binding pocket and provides insight into the ability of this site to recognize a variety of mannose-containing sugars.
About this Structure
1SZ0 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
The N-terminal carbohydrate recognition site of the cation-independent mannose 6-phosphate receptor., Olson LJ, Dahms NM, Kim JJ, J Biol Chem. 2004 Aug 6;279(32):34000-9. Epub 2004 May 28. PMID:15169779
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