Structure of the TRAIL-DR5 complex reveals mechanisms conferring specificity in apoptotic initiation

Nature Structural Biology

Volumn 6, Issue 11, 1999, Pages 1048-1053

  Mongkolsapaya, Juthathip ^a   Grimes, Jonathan M ^b   Chen, Nan ^a   Xu, Xiao Ning ^a   Stuart, David I ^b,c   Jones, E Yvonne ^b,c   Screaton, Gavin R ^a  

^a JOHN RADCLIFFE HOSPITAL   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE RECEPTOR; LIGAND;

AMINO ACID SEQUENCE; APOPTOSIS; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; APOPTOSIS; APOPTOSIS REGULATORY PROTEINS; CRYSTALLOGRAPHY, X-RAY; HUMANS; LIGANDS; MEMBRANE GLYCOPROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION; RECEPTORS, TNF-RELATED APOPTOSIS-INDUCING LIGAND; RECEPTORS, TUMOR NECROSIS FACTOR; SEQUENCE ALIGNMENT; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; TNF-RELATED APOPTOSIS-INDUCING LIGAND; TUMOR NECROSIS FACTOR-ALPHA;

EID: 0032750511     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/14935     Document Type: Article

References (31)

1. Nagata, S. Ce 88, 355-365 (1997).
2. Golstein, P. Curr-Biol7. R750-R753 (1997).
3. Wiley, S. Ret al. Immunity 3. 673-682 (1995).
4. Mongkolsapaya, J. et al. J-lmmunol 160, 3-6(1998).
5. Walczak, H. et al. Nature Med. 5, 157-163 (1999).
6. Jones. E. YStuart. D. I. Walker. N. P. Nature 338, 225-228 (1989).
7. Banner, D.W. et al. Cell 73, 431-445 (1993).
8. Karpusas, M. et al. Structures, 1031-1039(1995).
9. Cha, 5. 5. et al. Immunity 11, 253-261 (1999).
10. Naismith, J. HDevine, T. QKohno, T. Sprang, S. R. Structure 4, 1251-1262. (1996).
11. Yamagishi, J. et al. Protein Eng. 3, 713-719 (1990).
12. Goh, C. RLoh, C. S. Porter, A. G. Protein Eng. 4, 785-791 (1991).
13. Schneider, P. et al. J. Biol. Cfiem. 272. 18827-12833 (1997).
14. Brojatsch, JNaughton, JRolls, M. MZingler, K. Young, J. A. Cell 87, 845-855(1996).
15. Screaton, G. RMongkolsapaya, JXu, X. NCowper, A. EMcMichael, A. J. 8 Bell. J. I. Curr. Biol. 7, 693-696 (1997).
16. Park, Y. CBurkitt, VVilla, A. Rlong, L. Wu, H Nature 398, 533-538 (1999).
17. Gao. G. F. et al. Protein Sci. 7, 1245-1249(1998).
18. Cordingley, M. GCallahan, P. L, Sardana, V. VGarsky, V. M. Colonno, R. J. J. Biol. Chem. 265, 9062-9065 (1990).
19. Otwinowskr, Z. O. Minor, W. Methods Enzymol. 276, 307-326 (1997).
20. Navaza.J. Acta.Crystallogr.A50, 157-163(1994).
21. Brünger, A. T. XPLOK Version 3.1: A system for X-ray Crystallography and NMK. (Yale University Press New Haven, Connecticut; 1992).
22. Brunger, A. T. et al. Acta. Crystallogr. D 54, 905-921 (1998).
23. Collaborative Computational Project, No. 4 Acta Crystallogr D 50: 760-763 (1994).
24. De La Fortelle. E. Bricogne. G. Meth. Enzymol. 276. 442-494 (1997).
25. Jones, T. AZou, J. Y. Cowan, S. W. Kjeldgaard, M. Acta. Crystallogr. A 47, 110-119(1991).
26. Stuart, D. lLevine. MMuirhead. H. Stammers, D. K. J. Mol. Biol 134, 109-142(1979).
27. Hubbard, S. J. Thornton, J. M. A/access, computer program. (University College, London; 1993).
28. Esnouf, R. M. Acta. Crystallogr. D 55, 938-940 (1999).
29. Merritt, E. A. Bacon, D. J. Methods Enzymol. 277, 505-524 (1997).
30. Van Ostade. XTavernier. J. Fiers, W. Protein Eng. 7, 5-22 (1994).
31. Nicholls, ASharp, K. A. Honig, B. Proteins 11, 281-295 (1991).