Structure of C8α-MACPF reveals mechanism of membrane attack in complement immune defense

Science

Volumn 317, Issue 5844, 2007, Pages 1552-1554

  Hadders, Michael A ^a   Beringer, Dennis X ^a   Gros, Piet ^a  

^a UTRECHT UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENT 8 ALPHA; COMPLEMENT COMPONENT C9; COMPLEMENT MEMBRANE ATTACK COMPLEX; CYTOLYSIN; UNCLASSIFIED DRUG; COMPLEMENT COMPONENT C8; CYTOTOXIN; MEMBRANE PROTEIN; PERFORIN; PORE FORMING CYTOTOXIC PROTEIN;

BACTERIUM; CRYSTAL STRUCTURE; CYTOLOGY; IMMUNE RESPONSE; MAMMAL; PROTEIN;

ANALYTIC METHOD; ARTICLE; CRYSTAL STRUCTURE; EVOLUTIONARY HOMOLOGY; HYDROPHOBICITY; IMMUNITY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; AMINO ACID SEQUENCE; CELL MEMBRANE; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; IMMUNOLOGY; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS); MAMMALIA;

AMINO ACID SEQUENCE; CELL MEMBRANE; COMPLEMENT C8; COMPLEMENT MEMBRANE ATTACK COMPLEX; CRYSTALLOGRAPHY, X-RAY; CYTOTOXINS; HUMANS; HYDROPHOBICITY; MEMBRANE GLYCOPROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PORE FORMING CYTOTOXIC PROTEINS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 34548670476     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1147103     Document Type: Article

References (32)

1. M. J. Walport, N. Engl. J. Med. 344, 1058 (2001).
2. M. J. Walport, N. Engl. J. Med. 344, 1140 (2001).
3. R. Wurzner, A. Orren, P. J. Lachmann, Immunodefic. Rev. 3, 123 (1992).
4. H. J. Muller-Eberhard, Annu. Rev. Immunol. 4, 503 (1986).
5. A. F. Esser, Toxicology 87, 229 (1994).
6. J. M. Sodetz, Curr. Top. Microbiol. Immunol. 140, 19 (1989).
7. E. W. Steckel, B. E. Welbaum, J. M. Sodetz, J. Biol. Chem. 258, 4318 (1983).
8. M. C. Peitsch et al., Mol. Immunol. 27, 589 (1990).
9. A. P. Gee, M. D. Boyle, T. Borsos, J. Immunol. 124, 1905 (1980).
10. J. Tschopp, H. J. Muller-Eberhard, E. R. Podack, Nature 298, 534 (1982).
11. J. Tschopp, J. Biol. Chem. 259, 7857 (1984).
12. R. G. DiScipio, T. E. Hugli, J. Biol. Chem. 260, 14802 (1985).
13. Y. Huang, F. Qiao, R. Abagyan, S. Hazard, S. Tomlinson, J. Biol. Chem. 281, 27398 (2006).
14. E. R. Podack, G. Dennert, Nature 302, 442 (1983).
15. G. Dennert, E. R. Podack, J. Exp. Med. 157, 1483 (1983).
16. E. R. Podack, H. Hengartner, M. G. Lichtenheld, Annu. Rev. Immunol. 9, 129 (1991).
17. D. J. Slade, B. Chiswell, J. M. Sodetz, Biochemistry 45, 5290 (2006).
18. J. Rossjohn, S. C. Feil, W. J. McKinstry, R. K. Tweten, M. W. Parker, Cell 89, 685 (1997).
19. G. Polekhina, K. S. Giddings, R. K. Tweten, M. W. Parker, Proc. Natl. Acad. Sci. U.S.A. 102, 600 (2005).
20. S. J. Tilley, H. R. Saibil, Curr. Opin. Struct. Biol. 16, 230 (2006).
21. R. K. Tweten, Infect. Immun. 73, 6199 (2005).
22. K. S. Giddings, J. Zhao, P. J. Sims, R. K. Tweten, Nat. Struct. Mol. Biol. 11, 1173 (2004).
23. M. W. Parker, S. C. Feil, Prog. Biophys. Mol. Biol. 88, 91 (2005).
24. L. A. Shepard et al., Biochemistry 37, 14563 (1998).
25. O. Shatursky et al., Cell 99, 293 (1999).
26. S. J. Tilley, E. V. Orlova, R. J. Gilbert, P. W. Andrew, H. R. Saibil, Cell 121, 247 (2005).
27. C. L. Brannen, J. M. Sodetz, Mol. Immunol. 44, 960 (2007).
28. D. H. Lockert et al., J. Biol. Chem. 270, 19723 (1995).
29. I. Voskoboinik et al., J. Biol. Chem. 280, 8426 (2005).
30. W. L. Delano, The PyMOL Molecular Graphics System (DeLano Scientific, San Carlos, CA, 2002), http://pymol.sourceforge.net.
31. Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
32. We thank T. H. C. Brondijk, B. J. C. Janssen, F. J. Milder, and L. Rutten for assistance, M. R. Daha, E. G. Huizinga and J. A. G. van Strijp for critically reading the manuscript. We thank the European Synchrotron Radiation Facility for providing synchrotron radiation facilities and the beamline scientists at ID-29 for their help with data collection. This work was supported by a "Pionier" grant (P.G.) of the Council for Chemical Sciences of the Netherlands Organization for Scientific Research. Coordinates and structure factors have been deposited in the Protein Data Bank (PDB) (www.rcsb.org) under accession code 2QQH.