rdf:type |
|
lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1996-8-22
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pubmed:abstractText |
Prespore-specific antigen (PsA) is a putative cell-adhesion molecule of the cellular slime mould Dictyostelium discoideum, which has a similar molecular architecture to several mammalian cell-surface proteins. It has an N-terminal globular domain presented to the extracellular environment on an O-glycosylated stem (glycopeptide) that is attached to the cell membrane through a glycosyl-PtdIns anchor. The sequence of PsA suggests that PsA may belong to a new family of cell-surface molecules and here we present information on the structure of the N-terminal globular domain and determine the reducing-terminal linkage of the O-glycosylation. To obtain a sufficient amount of pure protein, a secreted recombinant form of PsA (rPsA), was expressed in D. discoideum and characterised. 1H-NMR spectra of rPsA contained features consistent with a high degree of beta-sheet in the N-terminal globular domain, a feature commonly observed in cell-adhesion proteins. Solid-phase Edman degradation of the glycopeptide of rPsA indicated that 14 of the 15 threonines and serines in the spacer region were glycosylated. The chemical structures of the O-glycosylations were determined to be single N-acetylglucosamine residues.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetylglucosamine,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Protozoan,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin,
http://linkedlifedata.com/resource/pubmed/chemical/prespore-specific antigen...
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
|
pubmed:issn |
0014-2956
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pubmed:author |
pubmed-author:CurmiP MPM,
pubmed-author:GooleyA AAA,
pubmed-author:JardineD RDR,
pubmed-author:KarusoPP,
pubmed-author:MabbuttB CBC,
pubmed-author:MossC JCJ,
pubmed-author:PackerN HNH,
pubmed-author:SladeM BMB,
pubmed-author:TempleM DMD,
pubmed-author:WilliamsK LKL,
pubmed-author:ZacharaN ENE
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
238
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
511-8
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:8681966-Acetylglucosamine,
pubmed-meshheading:8681966-Amino Acid Sequence,
pubmed-meshheading:8681966-Animals,
pubmed-meshheading:8681966-Antigens, Protozoan,
pubmed-meshheading:8681966-Antigens, Surface,
pubmed-meshheading:8681966-Carbohydrate Conformation,
pubmed-meshheading:8681966-Chromatography, Gas,
pubmed-meshheading:8681966-Chromatography, High Pressure Liquid,
pubmed-meshheading:8681966-Dictyostelium,
pubmed-meshheading:8681966-Fungal Proteins,
pubmed-meshheading:8681966-Glycopeptides,
pubmed-meshheading:8681966-Glycosylation,
pubmed-meshheading:8681966-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8681966-Mass Spectrometry,
pubmed-meshheading:8681966-Membrane Glycoproteins,
pubmed-meshheading:8681966-Molecular Sequence Data,
pubmed-meshheading:8681966-Protein Structure, Secondary,
pubmed-meshheading:8681966-Protozoan Proteins,
pubmed-meshheading:8681966-Recombinant Proteins,
pubmed-meshheading:8681966-Sequence Homology, Amino Acid,
pubmed-meshheading:8681966-Trypsin
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pubmed:year |
1996
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pubmed:articleTitle |
Recombinant prespore-specific antigen from Dictyostelium discoideum is a beta-sheet glycoprotein with a spacer peptide modified by O-linked N-acetylglucosamine.
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pubmed:affiliation |
Macquarie University Centre for Analytical Biotechnology, Sydney, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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