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The cell surface antigen CD59 is an inhibitor of complement-mediated lysis and a member of the Ly6 superfamily (Ly6SF) of cysteine-rich cell-surface molecules whose sequences are related to those of snake venom neurotoxins. The three-dimensional solution structure of a recombinant form of the extracellular region of the molecule (residues 1-70 of the mature protein; sCD59) has been solved by 2D NMR methods. sCD59 is a relatively flat, disk-shaped molecule consisting of a two-standed beta-sheet finger loosely packed against a protein core formed by a three-stranded beta-sheet and a short helix. Structure calculations allowed an unambiguous assignment of the disulfide-bonded cysteine pairs as 3-26, 6-13, 19-39, 45-63, and 64-69. The topology of sCD59 is similar to that of the snake venom neurotoxins and consistent with an evolutionary relationship existing between the Ly6SF and the neurotoxins.


Journal article



Publication Date





4471 - 4482


Amino Acid Sequence, Antigens, CD, CD59 Antigens, Crystallization, Disulfides, Electrochemistry, Extracellular Space, Hydrogen Bonding, Magnetic Resonance Spectroscopy, Membrane Glycoproteins, Models, Molecular, Molecular Sequence Data, Molecular Structure, Neurotoxins, Protein Structure, Secondary, Recombinant Proteins, Snake Venoms, Solutions