1sz0: Difference between revisions

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{{Seed}}
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{{STRUCTURE_1sz0|  PDB=1sz0  |  SCENE=  }}  
{{STRUCTURE_1sz0|  PDB=1sz0  |  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===




==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.
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{{ABSTRACT_PUBMED_15169779}}


==About this Structure==
==About this Structure==
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[[Category: Mannose 6-phosphate]]
[[Category: Mannose 6-phosphate]]
[[Category: Receptor]]
[[Category: Receptor]]
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