Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Semrock

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 3 June 2005:
Vol. 308. no. 5727, p. 1373
DOI: 10.1126/science.308.5727.1373p

This Week in Science

Interleukin-2 (IL-2) is central to the immune response. It forms a complex with three cell surface receptors, IL-2R, IL-2R, and IL-2R, to form a complex that signals through activation of downstream tyrosine kinases, JAK3 and STAT. Rickert et al. (p. 1477) have determined a 2.8 angstrom crystal structure of a complex between IL-2 and IL-2R. The IL-2R structure lacks a classical cytokine receptor fold, and the docking mode with IL-2 is distinct from known cytokine recognition modes. The structure provides a framework for engineering of improved IL-2 therapeutics.





ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products