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.
The Structure of Interleukin-2 Complexed with Its Alpha Receptor
Mathias Rickert,*Xinquan Wang,*Martin J. Boulanger,Natalia Goriatcheva,K. Christopher Garcia
Interleukin-2 (IL-2) is an immunoregulatory cytokine that bindssequentially to the alpha (IL-2R), beta (IL-2Rß),and common gamma chain (c) receptor subunits. Here we presentthe 2.8 angstrom crystal structure of a complex between humanIL-2 and IL-2R, which interact in a docking mode distinct fromthat of other cytokine receptor complexes. IL-2R is composedof strand-swapped "sushi-like" domains, unlike the classicalcytokine receptor fold. As a result of this domain swap, IL-2Ruses a composite surface to dock into a groove on IL-2 thatalso serves as a binding site for antagonist drugs. With thiscomplex, we now have representative structures for each classof hematopoietic cytokine receptor–docking modules.
Departments of Microbiology and Immunology, and Structural Biology, Stanford University School of Medicine, 299 Campus Drive, Fairchild D319, Stanford, CA 94305–5124, USA.
* These authors contributed equally to this work.
To whom correspondence should be addressed. E-mail: kcgarcia{at}stanford.edu
Identification of CD25+ {gamma}{delta} T Cells As Fetal Thymus-Derived Naturally Occurring IL-17 Producers.
K. Shibata, H. Yamada, R. Nakamura, X. Sun, M. Itsumi, and Y. Yoshikai (2008)
J. Immunol.
181, 5940-5947
|Abstract »|Full Text »|PDF »
IL-2 Receptor {beta}-Chain Signaling Controls Immunosuppressive CD4+ T Cells in the Draining Lymph Nodes and Lung during Allergic Airway Inflammation In Vivo.
A. Doganci, R. Karwot, J. H. Maxeiner, P. Scholtes, E. Schmitt, M. F. Neurath, H. A. Lehr, I-C. Ho, and S. Finotto (2008)
J. Immunol.
181, 1917-1926
|Abstract »|Full Text »|PDF »
IL-15R{alpha} chaperones IL-15 to stable dendritic cell membrane complexes that activate NK cells via trans presentation.
E. Mortier, T. Woo, R. Advincula, S. Gozalo, and A. Ma (2008)
J. Exp. Med.
205, 1213-1225
|Abstract »|Full Text »|PDF »
Crystal Structure of the Interleukin-15{middle dot}Interleukin-15 Receptor {alpha} Complex: INSIGHTS INTO TRANS AND CIS PRESENTATION.
S. K. Olsen, N. Ota, S. Kishishita, M. Kukimoto-Niino, K. Murayama, H. Uchiyama, M. Toyama, T. Terada, M. Shirouzu, O. Kanagawa, et al. (2007)
J. Biol. Chem.
282, 37191-37204
|Abstract »|Full Text »|PDF »
The Existence of Multiple Conformers of Interleukin-21 Directs Engineering of a Superpotent Analogue.
K. Bondensgaard, J. Breinholt, D. Madsen, D. H. Omkvist, L. Kang, A. Worsaae, P. Becker, C. B. Schiodt, and S. A. Hjorth (2007)
J. Biol. Chem.
282, 23326-23336
|Abstract »|Full Text »|PDF »
Identification of Their Epitope Reveals the Structural Basis for the Mechanism of Action of the Immunosuppressive Antibodies Basiliximab and Daclizumab.
M. Binder, F.-N. Vogtle, S. Michelfelder, F. Muller, G. Illerhaus, S. Sundararajan, R. Mertelsmann, and M. Trepel (2007)
Cancer Res.
67, 3518-3523
|Abstract »|Full Text »|PDF »
Hot-spot mimicry of a cytokine receptor by a small molecule.
), beta (IL-2Rß), and common gamma chain (
c) receptor subunits. Here we present the 2.8 angstrom crystal structure of a complex between human IL-2 and IL-2R
To whom correspondence should be addressed. E-mail: 
