1ERG

THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE EXTRACELLULAR REGION OF THE COMPLEMENT REGULATORY PROTEIN, CD59, A NEW CELL SURFACE PROTEIN DOMAIN RELATED TO NEUROTOXINS

Summary for 1ERG

• Entry DOI: 10.2210/pdb1erg/pdb
• Descriptor: CD59 (1 entity in total)
• Functional Keywords: complement factor
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 8095.21

Authors

Kieffer, B.,Driscoll, P.C.,Campbell, I.D.,Willis, A.C.,Van Der Merwe, P.A.,Davis, S.J. (deposition date: 1993-12-13, release date: 1994-04-30, Last modification date: 2024-10-16)

Primary citation

Kieffer, B.,Driscoll, P.C.,Campbell, I.D.,Willis, A.C.,van der Merwe, P.A.,Davis, S.J.
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.
Biochemistry, 33:4471-4482, 1994

PubMed Abstract: 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.

PubMed: 7512825
DOI: 10.1021/bi00181a006

Experimental method

SOLUTION NMR