1sz0: Difference between revisions
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|PDB= 1sz0 |SIZE=350|CAPTION= <scene name='initialview01'>1sz0</scene>, resolution 2.10Å | |PDB= 1sz0 |SIZE=350|CAPTION= <scene name='initialview01'>1sz0</scene>, resolution 2.10Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=M6P:ALPHA-D-MANNOSE-6-PHOSPHATE'>M6P</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=OS:OSMIUM+ION'>OS</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= IGF2R, M6P ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | |GENE= IGF2R, M6P ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1q25|1Q25]], [[1syo|1SYO]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sz0 OCA], [http://www.ebi.ac.uk/pdbsum/1sz0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sz0 RCSB]</span> | |||
}} | }} | ||
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[[Category: Kim, J J.P.]] | [[Category: Kim, J J.P.]] | ||
[[Category: Olson, L J.]] | [[Category: Olson, L J.]] | ||
[[Category: | [[Category: lectin]] | ||
[[Category: | [[Category: mannose 6-phosphate]] | ||
[[Category: | [[Category: receptor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:48:52 2008'' | ||
Revision as of 23:48, 30 March 2008
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| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | IGF2R, M6P (Bos taurus) | ||||||
| Related: | 1Q25, 1SYO
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
N-terminal 3 domains of CI-MPR bound to mannose 6-phosphate
OverviewOverview
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 StructureAbout this Structure
1SZ0 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
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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