1syo

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|PDB= 1syo |SIZE=350|CAPTION= <scene name='initialview01'>1syo</scene>, resolution 2.20&Aring;
|PDB= 1syo |SIZE=350|CAPTION= <scene name='initialview01'>1syo</scene>, resolution 2.20&Aring;
|SITE=
|SITE=
-
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=M6P:ALPHA-D-MANNOSE-6-PHOSPHATE'>M6P</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
+
|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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>
|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]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1syo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1syo OCA], [http://www.ebi.ac.uk/pdbsum/1syo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1syo RCSB]</span>
}}
}}
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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: GOL]]
+
[[Category: lectin]]
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[[Category: M6P]]
+
[[Category: mannose 6-phosphate]]
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[[Category: NAG]]
+
[[Category: receptor]]
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[[Category: lectin; receptor; mannose 6-phosphate]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:11:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:48:45 2008''

Revision as of 20:48, 30 March 2008


PDB ID 1syo

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands: , , , ,
Gene: IGF2R, M6P (Bos taurus)
Related: 1Q25


Resources: FirstGlance, OCA, PDBsum, RCSB
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

1SYO 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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