Skip to main content

Thank you for visiting 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.

Chemical biology

Caught in the activation

A crystal structure reveals how a protein kinase is activated by the binding of a small molecule at a pocket far from the catalytic site. This opens the door to the design of modulators of protein phosphorylation.

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

Access options

Buy article

Get time limited or full article access on ReadCube.


All prices are NET prices.

Figure 1: Small-molecule activation of PDK1.


  1. Pawson, T. & Scott, J. D. Trends Biochem. Sci. 30, 286–290 (2005).

    CAS  Article  Google Scholar 

  2. Zhang, J., Yang, P. L. & Gray, N. S. Nature Rev. Cancer 9, 28–39 (2009).

    Article  Google Scholar 

  3. Engel, M. et al. EMBO J. 25, 5469–5480 (2006).

    CAS  Article  Google Scholar 

  4. Hindie, V. et al. Nature Chem. Biol. 5, 758–764 (2009).

    CAS  Article  Google Scholar 

  5. Huse, M. & Kuriyan, J. Cell 109, 275–282 (2002).

    CAS  Article  Google Scholar 

  6. Pellicena, P. & Kuriyan, J. Curr. Opin. Struct. Biol. 16, 702–709 (2006).

    CAS  Article  Google Scholar 

  7. Biondi, R. M. et al. EMBO J. 19, 979–988 (2000).

    CAS  Article  Google Scholar 

Download references

Author information

Authors and Affiliations


Rights and permissions

Reprints and Permissions

About this article

Cite this article

Liu, Y. Caught in the activation. Nature 461, 484–485 (2009).

Download citation

  • Published:

  • Issue Date:

  • DOI:


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