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Structure paper

TitleIntermonomer interactions are essential for lysosomal enzyme binding by the cation-dependent mannose 6-phosphate receptor.
Journal, issue, pagesBiochemistry, Vol. 49, Page 236-246, Year 2010
Publish dateOct 5, 2009 (structure data deposition date)
AuthorsOlson, L.J. / Sun, G. / Bohnsack, R.N. / Peterson, F.C. / Dahms, N.M. / Kim, J.J.
External linksBiochemistry / PubMed:19928875
MethodsX-ray diffraction
Resolution1.9 - 2.3 Å
Structure data

PDB-3k41:
Crystal structure of sCD-MPR mutant E19Q/K137M bound to Man-6-P
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-3k42:
Crystal structure of sCD-MPR mutant E19Q/K137M pH 7.0
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-3k43:
Crystal structure of sCD-MPR mutant E19Q/K137M pH 6.5
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-M6D:
6-O-phosphono-beta-D-mannopyranose

ChemComp-HOH:
WATER

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-1GP:
SN-GLYCEROL-1-PHOSPHATE

ChemComp-SO4:
SULFATE ION

ChemComp-ACT:
ACETATE ION

ChemComp-IMD:
IMIDAZOLE

Source
  • bos taurus (cattle)
KeywordsProtein transport / sugar binding protein / transport / lysosome / mannose / receptor / sugar binding / Glycoprotein / Membrane / Phosphoprotein / Transmembrane

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