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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Harrison, R. A. Fletcher, C. M. Lachmann, P. J. Neuhaus, D. |
| Description | Country affiliation: United kingdom Author Affiliation: Fletcher CM ( MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.) |
| Abstract | 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. |
| ISSN | 09618368 |
| e-ISSN | 1469896X |
| Journal | Protein Science |
| Issue Number | 12 |
| Volume Number | 2 |
| Language | English |
| Publisher | Wiley-Blackwell (on behalf of The Protein Society) |
| Publisher Date | 1993-12-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Antigens, Cd Chemistry Glycoproteins Membrane Glycoproteins Antigens, Cd59 Carbohydrate Conformation Carbohydrate Sequence Magnetic Resonance Spectroscopy Molecular Sequence Data Protein Structure, Secondary Structure-activity Relationship Urine Comparative Study Research Support, Non-u.s. Gov't Discipline Biochemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Molecular Biology Biochemistry |
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