1m6p
From Proteopedia
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|PDB= 1m6p |SIZE=350|CAPTION= <scene name='initialview01'>1m6p</scene>, resolution 1.8Å | |PDB= 1m6p |SIZE=350|CAPTION= <scene name='initialview01'>1m6p</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=M6P:ALPHA-D-MANNOSE-6-PHOSPHATE'>M6P</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m6p OCA], [http://www.ebi.ac.uk/pdbsum/1m6p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m6p RCSB]</span> | ||
}} | }} | ||
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[[Category: Roberts, D L.]] | [[Category: Roberts, D L.]] | ||
[[Category: Weix, D J.]] | [[Category: Weix, D J.]] | ||
| - | [[Category: M6P]] | ||
| - | [[Category: MN]] | ||
[[Category: cation dependent mannose 6-phosphate]] | [[Category: cation dependent mannose 6-phosphate]] | ||
[[Category: p-type lectin]] | [[Category: p-type lectin]] | ||
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[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:12:04 2008'' |
Revision as of 19:12, 30 March 2008
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| , resolution 1.8Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
EXTRACYTOPLASMIC DOMAIN OF BOVINE CATION-DEPENDENT MANNOSE 6-PHOSPHATE RECEPTOR
Overview
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.
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
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