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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
14
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pubmed:dateCreated |
1989-6-30
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pubmed:abstractText |
The interactions of the bovine cation-dependent mannose 6-phosphate receptor with monovalent and divalent ligands have been studied by equilibrium dialysis. This receptor appears to be a homodimer or a tetramer. Each mole of receptor monomer bound 1.2 mol of the monovalent ligands, mannose 6-phosphate and pentamannose phosphate with Kd values of 8 X 10(-6) M and 6 X 10(-6) M, respectively and 0.5 mol of the divalent ligand, a high mannose oligosaccharide with two phosphomonoesters, with a Kd of 2 X 10(-7) M. When Mn2+ was replaced by EDTA in the dialysis buffer, the Kd for pentamannose phosphate was 2.5 X 10(-5) M. By measuring the affinity of the cation-dependent and cation-independent mannose 6-phosphate receptors for a variety of mannose 6-phosphate analogs, we conclude that the 6-phosphate and the 2-hydroxyl of mannose 6-phosphate each contribute approximately 4-5 kcal/mol of Gibb's free energy to the binding reaction. Neither receptor appears to interact substantially with the anomeric oxygen of mannose 6-phosphate. The receptors differ in that the cation-dependent receptor displays no detectable affinity for N-acetylglucosamine 1'-(alpha-D-methylmannopyranose 6-monophosphate) whereas this ligand binds to the cation-independent receptor with a poor, but readily measurable Kd of about 0.1 mM. The spacing of the mannose 6-phosphate-binding sites relative to each other may also differ for the two receptors.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetylglucosamine,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent,
http://linkedlifedata.com/resource/pubmed/chemical/Chlorides,
http://linkedlifedata.com/resource/pubmed/chemical/Edetic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Manganese,
http://linkedlifedata.com/resource/pubmed/chemical/Manganese Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Mannans,
http://linkedlifedata.com/resource/pubmed/chemical/Mannosephosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, IGF Type 2,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/manganese chloride,
http://linkedlifedata.com/resource/pubmed/chemical/mannose-6-phosphate,
http://linkedlifedata.com/resource/pubmed/chemical/methyl...,
http://linkedlifedata.com/resource/pubmed/chemical/pentamannose phosphate
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
264
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7970-5
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2542255-Acetylglucosamine,
pubmed-meshheading:2542255-Animals,
pubmed-meshheading:2542255-Binding Sites,
pubmed-meshheading:2542255-Cations, Divalent,
pubmed-meshheading:2542255-Cattle,
pubmed-meshheading:2542255-Chlorides,
pubmed-meshheading:2542255-Dialysis,
pubmed-meshheading:2542255-Edetic Acid,
pubmed-meshheading:2542255-Macromolecular Substances,
pubmed-meshheading:2542255-Manganese,
pubmed-meshheading:2542255-Manganese Compounds,
pubmed-meshheading:2542255-Mannans,
pubmed-meshheading:2542255-Mannosephosphates,
pubmed-meshheading:2542255-Oligosaccharides,
pubmed-meshheading:2542255-Receptor, IGF Type 2,
pubmed-meshheading:2542255-Receptors, Cell Surface,
pubmed-meshheading:2542255-Thermodynamics
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pubmed:year |
1989
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pubmed:articleTitle |
Ligand interactions of the cation-dependent mannose 6-phosphate receptor. Comparison with the cation-independent mannose 6-phosphate receptor.
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pubmed:affiliation |
Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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