Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Letter
  • Published:

Solution structure of a baculoviral inhibitor of apoptosis (IAP) repeat

Nature Structural Biology volume 6, pages 648–651 (1999)Cite this article

Abstract

Members of the inhibitor of apoptosis (IAP) family of proteins are able to inhibit cell death following viral infection, during development or in cell lines in vitro. All IAP proteins bear one or more baculoviral IAP repeats (BIRs). Here we describe the solution structure of the third BIR domain from the mammalian IAP homolog B (MIHB /c- IAP-1). The BIR domain has a novel fold that is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues. The structure consists of a series of short α-helices and turns with the zinc packed in an unusually hydrophobic environment created by residues that are highly conserved among all BIRs.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Figure 1: Domain structure of MIHB and BIR sequence alignment.
Figure 2: Structure of BIR3 from MIHB.
Figure 3: Stereo view of the zinc site from the structure closest to the geometric average of BIR3.

Similar content being viewed by others

Accession codes

Accessions

Protein Data Bank

References

  1. Crook, N.E., Clem, R.J. & Miller, L.K. J. Virol. 67, 2168– 2174 (1993).

    CAS  PubMed  PubMed Central  Google Scholar 

  2. Duckett, C.S. et al. EMBO J. 15, 2685–2694 (1996).

    Article  CAS  Google Scholar 

  3. Hay, B.A., Wassarman, D.A. & Rubin, G.M. Cell 83, 1253– 1262 (1995).

    Article  CAS  Google Scholar 

  4. Liston, P. et al. Nature 379, 349–353 (1996).

    Article  CAS  Google Scholar 

  5. Uren, A.G., Pakusch, M., Hawkins, C.J., Puls, K.L. & Vaux, D.L. Proc. Natl. Acad. Sci. USA 93, 4974–4978 (1996).

    Article  CAS  Google Scholar 

  6. Uren, A.G., Coulson, E.J. & Vaux, D.L. Trends Biochem. Sci. 23, 159 –162 (1998).

    Article  CAS  Google Scholar 

  7. Clem, R.J. & Miller, L.K. Mol. Cell. Biol. 14 , 5212–5222 (1994).

    Article  CAS  Google Scholar 

  8. Hawkins, C.J., Uren, A.G., Hacker, G., Medcalf, R.L. & Vaux, D.L. Proc. Natl. Acad. Sci. USA 93, 13786–13790 (1996).

    Article  CAS  Google Scholar 

  9. Vucic, D., Kaiser, W.J., Harvey, A.J. & Miller, L.K. Proc. Natl. Acad. Sci. USA 94, 10183– 10188 (1997).

    Article  CAS  Google Scholar 

  10. Ambrosini, G., Adida, C. & Altieri, D.C. Nature Med. 3, 917– 921 (1997).

    Article  CAS  Google Scholar 

  11. Roy, N., Deveraux, Q.L., Takahashi, R., Salvesen, G.S. & Reed, J.C. EMBO J. 16, 6914–6925 (1997).

    Article  CAS  Google Scholar 

  12. Deveraux, Q.L., Takahashi, R., Salvesen, G.S. & Reed, J.C. Nature 388, 300–304 ( 1997).

    Article  CAS  Google Scholar 

  13. Manji, G.A., Hozak, R.R., Lacount, D.J. & Friesen, P.D. J. Virol. 71, 4509–4516 (1997).

    CAS  PubMed  PubMed Central  Google Scholar 

  14. Deveraux, Q.L. et al. EMBO J. 17, 2215– 2223 (1998).

    Article  CAS  Google Scholar 

  15. Rothe, M., Pan, M.G., Henzel, W.J., Ayres, T.M. & Goeddel, D.V. Cell 83, 1243– 1252 (1995).

    Article  CAS  Google Scholar 

  16. Vucic, D., Kaiser, W.J. & Miller, L.K. J. Biol. Chem. 273, 33915– 33921 (1998).

    Article  CAS  Google Scholar 

  17. Birnbaum, M.J., Clem, R.J. & Miller, L.K. J. Virol. 68, 2521– 2528 (1994).

    CAS  PubMed  PubMed Central  Google Scholar 

  18. Mackay, J.P. & Crossley, M. Trends Biochem. Sci. 23, 1–4 (1998).

    Article  CAS  Google Scholar 

  19. Berg, J.M. & Shi, Y.G. Science 271, 1081–1085 (1996).

    Article  CAS  Google Scholar 

  20. Holm, L. & Sander, C. J. Mol. Biol. 233, 123–138 (1993).

    Article  CAS  Google Scholar 

  21. Karlin, S. & Zhu, Z.Y. Proc. Natl. Acad. Sci. USA 94, 14231–14236 (1997).

    Article  CAS  Google Scholar 

  22. Vucic, D., Kaiser, W.J. & Miller, L.K. Mol. Cell. Biol. 18, 3300– 3309 (1998).

    Article  CAS  Google Scholar 

  23. McCarthy, J.V. & Dixit, V.M. J. Biol. Chem. 273, 24009–24015 ( 1998).

    Article  CAS  Google Scholar 

  24. Eberstadt, M. et al. Nature 392, 941–945 (1998).

    Article  CAS  Google Scholar 

  25. Chou, J.J., Matsuo, H., Duan, H. & Wagner, G. Cell 94, 171–180 (1998).

    Article  CAS  Google Scholar 

  26. Huang, B.H., Eberstadt, M., Olejniczak, E.T., Meadows, R.P. & Fesik, S.W. Nature 384, 638–641 (1996).

    Article  CAS  Google Scholar 

  27. Clore, G.M. & Gronenborn, A.M. Nature Struct. Biol. (Suppl.) 4, 849–853 ( 1997).

    CAS  Google Scholar 

  28. Luginbühl, P., Szyperski, T. & Wüthrich, K. J. Magn. Reson. Series B 109, 229–233 (1995).

    Article  Google Scholar 

  29. Ludvigsen, S. & Poulsen, F.M. J. Biomol. NMR 2, 227–233 (1992).

    Article  CAS  Google Scholar 

  30. Güntert, P., Mumenthaler, C. & Wüthrich, K. J. Mol. Biol. 273, 283– 298 (1997).

    Article  Google Scholar 

  31. Brünger, A.T. X–PLOR version 3.851. A system for X–ray crystallography and NMR. (Yale University Press, New Haven, Connecticut; 1996 ).

    Google Scholar 

  32. Hinds, M.G., Maurer, T., Zhang, J.G., Nicola, N.A. & Norton, R.S. J. Biol. Chem. 273, 13738– 13745 (1998).

    Article  CAS  Google Scholar 

  33. Mackerell, A.D. et al. J. Phys. Chem. B 102, 3586– 3616 (1998).

    Article  CAS  Google Scholar 

  34. Laskowski, R.A., Rullmann, J.A.C., MacArthur, M.W., Kaptein, R. & Thornton, J.M. J. Biomol. NMR 8, 477–486 (1996).

    Article  CAS  Google Scholar 

  35. Koradi, R., Billeter, M. & Wüthrich, K. J. Mol. Graphics 14, 51– 55 (1996).

    Article  CAS  Google Scholar 

Download references

Acknowledgements

We wish to thank L. Miller for providing a preprint of a mutagenesis paper. This work was supported in part by a grant from the Australian Government (National Health and Medical Research Council) to D.L.V., the CRC for Cellular Growth Factors and grants to C.L.D from FRST (New Zealand) and the Marsden Fund (New Zealand).

Author information

Authors and Affiliations

  1. Biomolecular Research Institute, 343 Royal Parade, Parkville, 3052, Australia

    Mark G. Hinds & Raymond S. Norton

  2. The Cooperative Research Centre for Cellular Growth Factors.,

    Mark G. Hinds, Raymond S. Norton & David L. Vaux

  3. The Walter and Eliza Hall Institute of Medical Research, Post Office, Royal Melbourne Hospital, Parkville, 3050, Australia

    David L. Vaux

  4. Institute of Molecular BioSciences, Massey University, Palmerston North, New Zealand

    Catherine L. Day

Authors
  1. Mark G. Hinds
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Raymond S. Norton
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. David L. Vaux
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Catherine L. Day
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Catherine L. Day.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Hinds, M., Norton, R., Vaux, D. et al. Solution structure of a baculoviral inhibitor of apoptosis (IAP) repeat . Nat Struct Mol Biol 6, 648–651 (1999). https://doi.org/10.1038/10701

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/10701

This article is cited by

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing