Solution structure of the isolated Pelle death domain

FEBS Letters

Volumn 579, Issue 18, 2005, Pages 3920-3926

  Moncrieffe, Martin C ^a   Stott, Katherine M ^a   Gay, Nicholas J ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Death domains; NMR; Pelle; Tube

Indexed keywords

PROTEIN; PROTEIN KINASE; PROTEIN PELLE; PROTEIN TUBE; UNCLASSIFIED DRUG;

ARTICLE; CELL STRAIN; COMPARATIVE STUDY; CRYSTAL STRUCTURE; NUCLEAR MAGNETIC RESONANCE; PLASTICITY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN ISOLATION; PROTEIN PROTEIN INTERACTION; STRUCTURE ANALYSIS;

ANIMALS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; DROSOPHILA; DROSOPHILA PROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; ULTRACENTRIFUGATION;

EID: 22044456815     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.06.009     Document Type: Article

References (46)

1. M.P. Belvin, and K.V. Anderson A conserved signaling pathway: the Drosophila toll-dorsal pathway Annu. Rev. Cell Dev. Biol. 12 1996 393 416
2. J.L. Imler, and J.A. Hoffmann Signaling mechanisms in the antimicrobial host defense of Drosophila Curr. Opin. Microbiol. 3 2000 16 22
3. S. Rutschmann, A.C. Jung, C. Hetru, J.M. Reichahart, J.A. Hoffmann, and D. Ferrandon The Rel protein DIF mediates the antifungal but not the antibacterial host defense in Drosophila Immunity 12 2000 569 580
4. B. Beutler Endotoxin, Toll-like receptor 4 and the afferent limb of innate immunity Curr. Opin. Microbiol. 3 2000 23 28
5. K.V. Anderson, and C. Nüsslein-Volhard Information for the dorsal-ventral pattern of the Drosophila embryo is stored as maternal mRNA Nature 311 1984 223 227
6. P.M. Hecht, and K.V. Anderson Genetic characterization of tube and pelle, genes required for signalling between toll and dorsal in the specification of dorsal-ventral pattern of the Drosophila embryo Genetics 135 1993 407 417
7. D.N. Edwards, P. Towb, and S.A. Wasserman An activity-dependent network of interactions links the Rel protein Dorsal with its cytoplasmic regulators Development 124 1997 3855 3864
8. T. Horng, and R. Medzhitov Drosophila MyD88 is an adapter in the Toll signaling pathway Proc. Natl. Acad. Sci. USA 98 2001 12654 12658
9. S. Tauszig-Delamasure, H. Bilak, M. Capovilla, J.A. Hoffmann, and J.L. Imler Drosophila MyD88 is required for the response to fungal and Gram-positive bacterial infections Nat. Immunol. 3 2002 91 97
10. H. Sun, B.N. Bristow, Q. Guowei, and S.A. Wasserman A heterotrimeric death domain complex in Toll signaling Proc. Natl. Acad. Sci. USA 99 2002 12871 12876
11. C. Iphigenie, S. Luschnig, S. Bartoszewski, C. Nüsslein-Volhard, and B. Moussian Krapfen/dMyd88 is required for the establishment of dorsoventral pattern in Drosophila embryo Mech. Dev. 120 2003 219 226
12. Z. Cao, W.J. Henzel, and X. Gao IRAK: a kinase associated with the interleukin-1 receptor Science 271 1996 1128 1131
13. M. Muzio, J. Ni, P. Feng, and V.M. Dixit IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling Science 278 1997 1612 1615
14. S. Li, A. Strelow, E.J. Fontana, and H. Wesche IRAK-4: a novel member of the IRAK family with the properties of an IRAK-kinase Proc. Natl. Acad. Sci. USA 99 2002 5567 5572
15. K. Burns, F. Martinon, C. Esslinger, H. Pahl, P. Schneider, J.L. Bodmer, F.D. Marco, L. French, and J. Tschopp MyD88, an adapter protein involved in interleukin-1 signaling J. Biol. Chem. 273 1998 12203 12209
16. H. Wesche, W. Henzel, W. Shillinglaw, S. Li, and Z. Cao MyD88: an adapter that recruits IRAK to the IL-1 receptor complex Immunity 7 1997 837 847
17. L. Aravind, V.M. Dixit, and E.V. Koonin The domains of death: evolution of the apotosis machinery Trends Biochem. Sci. 24 1999 47 53
18. S.W. Fesik Insights into programmed cell death through structural biology Cell 103 2000 273 282
19. J.M. Hill, H. Vaidyanathan, J.W. Ramos, M.H. Ginsberg, and M.H. Werner Recognition of ERK MAP kinase by PEA-15 reveals a common docking site within the death domain and death effector domain EMBO J. 21 2002 6494 6504
20. T. Xiao, P. Towb, S.A. Wasserman, and S.R. Sprang Three-dimensional structure of a complex between the death domains of Pelle and Tube Cell 99 1999 545 555
21. D.A. Schiffmann, J.H.M. White, A. Cooper, M.A. Nutley, S.E. Harding, K. Jumel, R. Solari, K.P. Ray, and N.J. Gay Formation and biochemical characterization of Tube/Pelle death domain complexes: critical regulators of postreceptor signaling by drosophila toll receptor Biochemistry 38 1999 11722 11733
22. H. Qin, S.M. Srinivasula, G. Wu, T. Fernandes-Alnemri, E.S. Alnemri, and Y. Shi Structural basis of Procaspase-9 recruitment by the apoptotic protease-activating factor 1 Nature 399 1999 459 557
23. C.H. Weber, and C. Vincenz The death domain superfamily: a tale of two interfaces? Trends Biochem. Sci. 26 2001 475 481
24. F.C. Neidhardt, P.L. Bloch, and D.F. Smith Culture medium for Enterobacteria J. Bacteriol. 119 1974 736 747
25. N. Sreerama, V.S. Yu, and R.W. Woody Estimation of the number of α-helical and β-strand segments in proteins using CD spectroscopy Prot. Sci. 8 1999 370 380
26. K. Pervushin, R. Riek, G. Wider, and K. Wúthrich Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules insolution Proc. Natl. Acad. Sci. USA 94 1997 12366 12371
27. Boucher, W. The Azara suite of programs version 2.7.
28. P.J. Kraulis, P.J. Domaille, S.L. Campbell-Burk, T. van Aken, and E.D. Laue Solution structure and dynamics of Ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy Biochemistry 33 1994 3515 3531
29. S. Grzesiek, and A. Bax Improved 3D tripple-resonance NMR techniques applied to a 31 kDa protein J. Magn. Reson. 96 1992 432 440
30. 15N-enriched proteins J. Am. Chem. Soc. 115 1993 7772 7777
31. S. Grzesiek, and A. Bax Correlating backbone amide and side chain resonances in larger proteins by multiple relayed tripple resonance NMR J. Am. Chem. Soc. 114 1992 6291 6293
32. G.T. Montelione, B.A. Lyons, S.D. Emerson, and M. Tashiro An efficient triple resonance experiment using Carbon-13 isotropic mixing for determining sequence-specific resonance assignments of isotopically-enriched proteins J. Am. Chem. Soc. 114 1992 10974 10975
33. 13C resonances of interleukin-1β using double- and triple-resonance heteronuclear three-dimensional NMR spectrosscopy Biochemistry 29 1990 8172 8184
34. 15N labelled proteins J. Am. Chem. Soc. 111 1989 1515 1517
35. L.E. Kay, D. Marion, and A. Bax Practical aspects of 3D heteronuclear NMR of proteins J. Mag. Reson. 84 1989 72 84
36. 13C-labelled protein J. Mag. Reson. 86 1990 204 209
37. G. Cornilescu, F. Delaglio, and A. Bax Protein backbone angle restraints from searching a database for chemical shift and sequence homology J. Biomol. NMR 13 1999 289 302
38. A.T. Brünger, P.D. Adams, G.M. Clore, W.L. DeLano, P. Gros, R.W. Grosse-Kunstleve, J.-S. Jiang, J. Kuszewski, N. Nigles, N.S. Pannu, R.J. Read, L.M. Rice, T. Simonson, and G.L. Warren Crystallography and NMR system (CNS): a new software system for macromolecular structure determination Acta Cryst. D54 1998 905 921
39. J.P. Linge, S.I. O'Donoghue, and M. Nigles Assigning ambiguous NOEs with ARIA Methods Enzymol. 339 2001 71 90
40. R.A. Laskowski, J.A. Rullmann, J.A. MacArthur, R. Kaptein, and J.M. Thornton AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8 1996 477 486
41. T.M. Laue, B.D. Shah, T.M. Ridgeway, and S.L. Pelletier Computer-aided interpretation of analytical sedimentation data for proteins S.E. Harding A.J. Rowe J.C. Horton Analytical ultracentrifugation in biochemistry and polymer science 1992 The Royal Society of Chemistry Cambridge, UK 90 125
42. P. Schuck Size distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling Biophys. J. 78 2000 1606 1619
43. T. Xiao, K.H. Gardner, and S.R. Sprang Cosolvent-induced transformation of a death domain tertiary structure Proc. Natl. Acad. Sci. USA 99 2002 11151 11156
44. E. Feinstein, A. Kimchi, D. Wallach, M. Boldin, and E. Varfolomeev The death domain: a module shared by proteins with diverse cellular functions Trends Biochem. Sci. 20 1995 342 344
45. J.M. Word, S.C. Lovell, T.H. LaBean, H.C. Taylor, M.E. Zalis, B.K. Presly, J.S. Richardson, and D.C. Richardson Visualizing and quantifying molecular goodness-of-fit: small-probe contact dots with explicit hydrogen atoms J. Mol. Biol. 285 1999 1711 1733
46. D.S. Wishart, B.D. Sykes, and F.M. Richards Relationship between NMR chemical-shift and protein secondary structure Mol. Cell Biol. 222 1991 311 333