Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain
10.1038/35050006
Crossref journal-article
Springer Science and Business Media LLC
Nature (297)
Authors 9
  1. Zhihong Liu (first)
  2. Chaohong Sun (additional)
  3. Edward T. Olejniczak (additional)
  4. Robert P. Meadows (additional)
  5. Stephen F. Betz (additional)
  6. Thorsten Oost (additional)
  7. Julia Herrmann (additional)
  8. Joe C. Wu (additional)
  9. Stephen W. Fesik (additional)
References 27 Referenced 530
  1. Crook, N. E., Clem, R. J. & Miller, L. K. An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif. J. Virol. 67, 2168–2174 (1993). (10.1128/JVI.67.4.2168-2174.1993) / J. Virol. by NE Crook (1993)
  2. Hawkins, C. J., Uren, A. G., Häcker, G., Medcalf, R. L. & Vaux, D. L. Inhibition of interleukin 1β-converting enzyme-mediated apoptosis of mammalian cells by baculovirus IAP. Proc. Natl Acad. Sci. USA 93, 13786–13790 (1996). (10.1073/pnas.93.24.13786) / Proc. Natl Acad. Sci. USA by CJ Hawkins (1996)
  3. Deveraux, Q. L., Takahashi, R., Salvesen, G. S. & Reed, J. C. X-linked IAP is a direct inhibitor of cell-death proteases. Nature 388, 300–304 (1997). (10.1038/40901) / Nature by QL Deveraux (1997)
  4. Roy, N., Deveraux, Q. L., Takahashi, R., Salvesen, G. S. & Reed, J. C. The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases. EMBO J. 16, 6914–6925 (1997). (10.1093/emboj/16.23.6914) / EMBO J. by N Roy (1997)
  5. Deveraux, Q. L. et al. Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases. EMBO J. 18, 5242–5251 (1999). (10.1093/emboj/18.19.5242) / EMBO J. by QL Deveraux (1999)
  6. Du, C., Fang, M., Li, Y., Li, L. & Wang, X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 102, 33–42 (2000). (10.1016/S0092-8674(00)00008-8) / Cell by C Du (2000)
  7. Verhagen, A. M. et al. Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell 102, 43–53 (2000). (10.1016/S0092-8674(00)00009-X) / Cell by AM Verhagen (2000)
  8. Srinivasula, S. M. et al. Molecular determinants of the caspase-promoting activity of Smac/DIABLO and its role in the death receptor pathway. J. Biol. Chem. 275, 36152–36157 (2000). (10.1074/jbc.C000533200) / J. Biol. Chem. by SM Srinivasula (2000)
  9. Chai, J. et al. Structural and biochemical basis of apoptotic activation by Smac/DIABLO. Nature 406, 855–862 (2000). (10.1038/35022514) / Nature by J Chai (2000)
  10. Tamm, I. et al. Expression and prognostic significance of IAP-family genes in human cancers and myeloid leukemias. Clin. Cancer Res. 6, 1796–1803 (2000). / Clin. Cancer Res. by I Tamm (2000)
  11. Ambrosini, G., Adida, C. & Altieri, D. C. A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma. Nature Med. 3, 917–217 (1997). (10.1038/nm0897-917) / Nature Med. by G Ambrosini (1997)
  12. LaCasse, E. C., Baird, S., Korneluk, R. G. & MacKenzie, A. E. The inhibitors of apoptosis (IAPs) and their emerging role in cancer. Oncogene 17, 3247–3259 (1998). (10.1038/sj.onc.1202569) / Oncogene by EC LaCasse (1998)
  13. Sun, C. et al. NMR structure and mutagenesis of the inhibitor-of-apoptosis protein XIAP. Nature 401, 818–822 (1999). (10.1038/44617) / Nature by C Sun (1999)
  14. Sun, C. et al. NMR structure and mutagenesis of the third BIR domain of the inhibitor of apoptosis protein XIAP. J. Biol. Chem. 275, 33777–33781 (1998). (10.1074/jbc.M006226200) / J. Biol. Chem. by C Sun (1998)
  15. Verdecia, M. A. et al. Structure of the human anti-apoptotic protein survivin reveals a dimeric arrangement. Nature Struct. Biol. 7, 602–608 (2000). (10.1038/77929) / Nature Struct. Biol. by MA Verdecia (2000)
  16. Muchmore, S. W. et al. Crystal structure and mutagenic analysis of the inhibitor-of-apoptosis protein survivin. Mol. Cell 6, 173–182 (2000). (10.1016/S1097-2765(05)00019-5) / Mol. Cell by SW Muchmore (2000)
  17. Chantalat, L. et al. Crystal structure of human survivin reveals a bow-tie-shaped dimer with two unusual α-helical extensions. Mol. Cell 6, 183–189 (2000). (10.1016/S1097-2765(05)00020-1) / Mol. Cell by L Chantalat (2000)
  18. Kleywegt, G. J. & Jones, T. A. in From First Map to Final Model (eds Bailey, S., Hubbard, R. & Waller, D.) 59–66 (Daresbury Laboratory, Daresbury, UK, 1994). / From First Map to Final Model by GJ Kleywegt (1994)
  19. Vucic, D., Kaiser, W. J. & Miller, L. K. Inhibitor of apoptosis proteins physically interact with and block apoptosis induced by Drosophila proteins Hid and Grim. Mol. Cell Biol. 18, 3300–3309 (1998). (10.1128/MCB.18.6.3300) / Mol. Cell Biol. by D Vucic (1998)
  20. Cutforth, T. & Gaul, U. A methionine aminopeptidase and putative regulator of translation initiation is required for cell growth and patterning in Drosophila. Mech. Dev. 82, 23–28 (1999). (10.1016/S0925-4773(99)00006-4) / Mech. Dev. by T Cutforth (1999)
  21. Clore, G. M. & Gronenborn, A. M. Multidimensional heteronuclear magnetic resonance of proteins. Methods Enzymol. 239, 349–363 (1994). (10.1016/S0076-6879(94)39013-4) / Methods Enzymol. by GM Clore (1994)
  22. Cornilescu, G., Delaglio, F. & Bax, A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289–302 (1999). (10.1023/A:1008392405740) / J. Biomol. NMR by G Cornilescu (1999)
  23. Stein E. G., Rice, L. M. & Brünger, A. T. Torsion-angle molecular dynamics as a new efficient tool for NMR structure calculation. J. Magn. Reson. B 124, 154–164 (1997). (10.1006/jmre.1996.1027) / J. Magn. Reson. B by Stein E. G. (1997)
  24. Nilges, M., Gronenborn, A. M., Brünger, A. T. & Clore, G. M. Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2. Protein Eng. 2, 27–38 (1988). (10.1093/protein/2.1.27) / Protein Eng. by M Nilges (1988)
  25. Nilges, M., Macias, M. J., O'Donoghue, S. I. & Oschkinat, H. Automated NOESY interpretation with ambiguous distance restraints: The refined NMR solution structure of the pleckstrin homology domain from β-spectrin. J. Mol. Biol. 269, 408–422 (1997). (10.1006/jmbi.1997.1044) / J. Mol. Biol. by M Nilges (1997)
  26. Laskowski, R. A., Rullmann, J. A., MacArthur, M. W., Kaptein, R. & Thornton, J. M. AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477–486 (1996). (10.1007/BF00228148) / J. Biomol. NMR by RA Laskowski (1996)
  27. Carson, M. J. Ribbon models of macromolecules. J. Mol. Graphics 5, 103–106 (1987). (10.1016/0263-7855(87)80010-3) / J. Mol. Graphics by MJ Carson (1987)
Dates
Type When
Created 23 years, 1 month ago (July 26, 2002, 4:46 a.m.)
Deposited 2 years, 3 months ago (May 16, 2023, 9:44 p.m.)
Indexed 2 weeks, 6 days ago (Aug. 12, 2025, 6:15 p.m.)
Issued 24 years, 9 months ago (Dec. 1, 2000)
Published 24 years, 9 months ago (Dec. 1, 2000)
Published Print 24 years, 9 months ago (Dec. 1, 2000)
Funders 0

None

@article{Liu_2000, title={Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain}, volume={408}, ISSN={1476-4687}, url={http://dx.doi.org/10.1038/35050006}, DOI={10.1038/35050006}, number={6815}, journal={Nature}, publisher={Springer Science and Business Media LLC}, author={Liu, Zhihong and Sun, Chaohong and Olejniczak, Edward T. and Meadows, Robert P. and Betz, Stephen F. and Oost, Thorsten and Herrmann, Julia and Wu, Joe C. and Fesik, Stephen W.}, year={2000}, month=dec, pages={1004–1008} }