Three-dimensional solution structure of the extracellular region of the complement regulatory protein CD59, a new cell-surface protein domain related to snake venom neurotoxins.

Journal article

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.

Authors: Kieffer, B; Driscoll, P; Campbell, I; Willis, A; Van Der Merwe, P

• Publication status: Published
• Journal: Biochemistry
• Volume: 33
• Issue: 15
• Pages: 4471-4482
• Publication date: 1994-04-01
• DOI: 10.1021/bi00181a006
• EISSN: 1520-4995
• ISSN: 0006-2960
• Language: English
• Keywords: Membrane Glycoproteins; Solutions; Molecular Sequence Data; Models, Molecular; Recombinant Proteins; Antigens, CD; Disulfides; Protein Structure, Secondary; Crystallization; Hydrogen Bonding; Antigens, CD59; Snake Venoms; Magnetic Resonance Spectroscopy; Extracellular Space; Amino Acid Sequence; Molecular Structure; Neurotoxins; Electrochemistry