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.

  • News & Views
  • Published:

MEMBRANE PROTEINS

The band 3–ankyrin multiprotein complex comes in from the cold

Nature Structural & Molecular Biology volume 29, pages 621–623 (2022)Cite this article

Subjects

Two new papers describe the successful purification of the partially intact human native red blood cell band 3 multiprotein membrane complexes, providing information that the authors then use to capture the structures and interactions of multiple erythrocyte proteins using high-resolution cryo-EM.

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

Fig. 1: A cryo-EM map of the domain organizations of band 3 dimer, protein 4.2 and ankyrin.
Fig. 2: Cryo-EM density map of a B3 ankyrin complexes.

References

  1. Vallese, F. et al. Nat. Struct. Mol. Biol. https://doi.org/10.1038/s41594-022-00792-w (2022).

    Article  Google Scholar 

  2. Xia, X., Liu, S. & Hong Zhou, Z. Nat. Struct. Mol. Biol. https://doi.org/10.1038/s41594-022-00779-7 (2022).

    Article  PubMed  Google Scholar 

  3. Bruce, L. J. et al. Blood 101, 4180–4188 (2003).

    Article  CAS  Google Scholar 

  4. van den Akker, E., Satchwell, T. J., Williamson, R. C. & Toye, A. M. Blood Cells Molec. Dis. 45, 1–8 (2010).

    Article  Google Scholar 

  5. Salomao, M. et al. Proc. Natl Acad. Sci. USA 105, 8026–8031 (2008).

    Article  CAS  Google Scholar 

  6. Perrotta, S., Gallagher, P. G. & Mohandas, N. Lancet 372, 1411–1426 (2008).

    Article  CAS  Google Scholar 

  7. Schofield, A. E., Reardon, D. M. & Tanner, M. J. A. Nature 355, 836–838 (1992).

    Article  CAS  Google Scholar 

  8. Bruce, L. J. Blood Cells Molec. Dis. 42, 216–222 (2009).

    Article  CAS  Google Scholar 

  9. Zhang, D., Kiyatkin, A., Bolin, J. T. & Low, P. S. Blood 96, 2925–2933 (2000).

    Article  CAS  Google Scholar 

  10. Arakawa, T. et al. Science 350, 680–684 (2015).

    Article  CAS  Google Scholar 

  11. Gruswitz, F. et al. Proc. Natl Acad. Sci. USA 107, 9638–9643 (2010).

    Article  CAS  Google Scholar 

  12. Toye, A. M. et al. Blood 105, 4088–4095 (2005).

    Article  CAS  Google Scholar 

  13. Mankelow, T. J., Satchwell, T. J. & Burton, N. M. Blood Cells Molec. Dis. 49, 1–10 (2012).

    Article  CAS  Google Scholar 

Download references

Acknowledgements

The author thanks H. Zhou and O. Clarke for their generation of Figs. 1 and 2, respectively, and T. Satchwell for critical reading of this article.

Author information

Authors and Affiliations

  1. University of Bristol, Biomedical Sciences Building, School of Biochemistry, Bristol, UK

    Ashley M. Toye

  2. Bristol Institute of Transfusion Sciences, NHS Blood and Transplant, Filton, Bristol, UK

    Ashley M. Toye

Authors
  1. Ashley M. Toye
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Ashley M. Toye.

Ethics declarations

Competing interests

The author declares no competing interests.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Toye, A.M. The band 3–ankyrin multiprotein complex comes in from the cold. Nat Struct Mol Biol 29, 621–623 (2022). https://doi.org/10.1038/s41594-022-00789-5

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/s41594-022-00789-5

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