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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
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Identification of Their Epitope Reveals the Structural Basis for the Mechanism of Action of the Immunosuppressive Antibodies Basiliximab and Daclizumab.
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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: 
