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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
1994-3-8
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pubmed:abstractText |
CD59 is a recently discovered cell-surface glycoprotein that restricts lysis by homologous complement and has limited sequence similarity to snake venom neurotoxins. This paper describes the first results of a two-dimensional NMR study of CD59 prepared from human urine. Nearly complete 1H-NMR assignments were obtained for the 77 amino acid residues and partial assignments for the N-glycan and the glycosylphosphatidylinositol (GPI) anchor. These results together confirm that the C-terminal residue of the mature protein is Asn 77 and that the urine-derived form retains the nonlipid part of the GPI anchor. The data further indicate that the GPI anchor and possibly the N-glycan are structurally inhomogeneous and suggest that the phospholipid present in the intact GPI anchor was removed by phosphatidylinositol-specific phospholipase-D. The folding topology of the protein was determined from NOE enhancements and slowly exchanging backbone amide protons and consists primarily of five extended strands (denoted beta 1-beta 5 in sequence order), arranged into separate two-stranded (beta 1 and beta 2) and three-stranded (beta 3-beta 5) antiparallel beta-sheets. The same folding topology is found in all of the snake venom neurotoxins whose structures have been determined. The region between the beta 4 and beta 5 strands has helical character, a feature that is not present in the neurotoxins but that is seen in the topologically similar wheat germ agglutinin.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507750-1317211,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507750-1370512,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/7507750-6340957,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507750-7236608,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507750-7682985,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507750-7915183,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507750-8443154
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0961-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2015-27
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7507750-Antigens, CD,
pubmed-meshheading:7507750-Antigens, CD59,
pubmed-meshheading:7507750-Base Sequence,
pubmed-meshheading:7507750-Carbohydrate Conformation,
pubmed-meshheading:7507750-Carbohydrate Sequence,
pubmed-meshheading:7507750-Glycoproteins,
pubmed-meshheading:7507750-Humans,
pubmed-meshheading:7507750-Magnetic Resonance Spectroscopy,
pubmed-meshheading:7507750-Membrane Glycoproteins,
pubmed-meshheading:7507750-Molecular Sequence Data,
pubmed-meshheading:7507750-Protein Structure, Secondary,
pubmed-meshheading:7507750-Structure-Activity Relationship,
pubmed-meshheading:7507750-Urine
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pubmed:year |
1993
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pubmed:articleTitle |
Sequence-specific 1H-NMR assignments and folding topology of human CD59.
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pubmed:affiliation |
MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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