1sz0: Difference between revisions

Revision as of 23:33, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1sz0.png

Template:STRUCTURE 1sz0

N-terminal 3 domains of CI-MPR bound to mannose 6-phosphateN-terminal 3 domains of CI-MPR bound to mannose 6-phosphate

Template:ABSTRACT PUBMED 15169779

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

Page seeded by OCA on Sun Jul 27 23:33:22 2008

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-'''N-terminal 3 domains of CI-MPR bound to mannose 6-phosphate'''
+===N-terminal 3 domains of CI-MPR bound to mannose 6-phosphate===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15169779}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15169779 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15169779}}
 ==About this Structure==
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 [[Category: Mannose 6-phosphate]]
 [[Category: Receptor]]
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