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1m6p

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{{STRUCTURE_1m6p| PDB=1m6p | SCENE= }}
{{STRUCTURE_1m6p| PDB=1m6p | SCENE= }}
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'''EXTRACYTOPLASMIC DOMAIN OF BOVINE CATION-DEPENDENT MANNOSE 6-PHOSPHATE RECEPTOR'''
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===EXTRACYTOPLASMIC DOMAIN OF BOVINE CATION-DEPENDENT MANNOSE 6-PHOSPHATE RECEPTOR===
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==Overview==
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Targeting of newly synthesized lysosomal hydrolases to the lysosome is mediated by the cation-dependent mannose 6-phosphate receptor (CD-MPR) and the insulin-like growth factor II/cation-independent mannose 6-phosphate receptor (IGF-II/CI-MPR). The two receptors, which share sequence similarities, constitute the P-type family of animal lectins. We now report the three-dimensional structure of a glycosylation-deficient, yet fully functional form of the extracytoplasmic domain of the bovine CD-MPR (residues 3-154) complexed with mannose 6-phosphate at 1.8 A resolution. The extracytoplasmic domain of the CD-MPR crystallizes as a dimer, and each monomer folds into a nine-stranded flattened beta barrel, which bears a striking resemblance to avidin. The distance of 40 A between the two ligand-binding sites of the dimer provides a structural basis for the observed differences in binding affinity exhibited by the CD-MPR toward various lysosomal enzymes.
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{{ABSTRACT_PUBMED_9604938}}
==About this Structure==
==About this Structure==
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[[Category: Receptor]]
[[Category: Receptor]]
[[Category: Transport]]
[[Category: Transport]]
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Revision as of 20:20, 2 July 2008

Image:1m6p.png

Template:STRUCTURE 1m6p

EXTRACYTOPLASMIC DOMAIN OF BOVINE CATION-DEPENDENT MANNOSE 6-PHOSPHATE RECEPTOR

Template:ABSTRACT PUBMED 9604938

About this Structure

1M6P is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Molecular basis of lysosomal enzyme recognition: three-dimensional structure of the cation-dependent mannose 6-phosphate receptor., Roberts DL, Weix DJ, Dahms NM, Kim JJ, Cell. 1998 May 15;93(4):639-48. PMID:9604938

Page seeded by OCA on Wed Jul 2 23:20:04 2008

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