1syo
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1syo.gif|left|200px]] | [[Image:1syo.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1syo", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | + | --> | |
- | + | {{STRUCTURE_1syo| PDB=1syo | SCENE= }} | |
- | + | ||
- | | | + | |
- | }} | + | |
'''N-terminal 3 domains of CI-MPR bound to mannose 6-phosphate''' | '''N-terminal 3 domains of CI-MPR bound to mannose 6-phosphate''' | ||
Line 28: | Line 25: | ||
[[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 Sat May 3 09:17:18 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 06:17, 3 May 2008
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 Page seeded by OCA on Sat May 3 09:17:18 2008