1. The structure of interleukin-2 complexed with its alpha receptor
- Author
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Rickert, Mathias, Wang, Xinquan, Boulanger, Martin J., Goriatcheva, Natalia, and Garcia, K. Christopher
- Subjects
Interleukin-2 -- Research -- Structure ,Science and technology ,Structure ,Research - Abstract
Intedeukin-2 (IL-2) is an immunoregulatory cytokine that binds sequentially to the alpha (IL-2Rα), beta (IL-2Rβ), and common gamma chain ([γ.sub.c]) receptor subunits. Here we present the 2.8 angstrom crystal structure of a complex between human IL-2 and IL-2Rα, which interact in a docking mode distinct from that of other cytokine receptor complexes. IL-2Rα is composed of strandswapped 'sushi-like' domains, unlike the classical cytokine receptor fold. As a result of this domain swap, IL-2Rα uses a composite surface to dock into a groove on IL-2 that also serves as a binding site for antagonist drugs. With this complex, we now have representative structures for each class of hematopoietic cytokine receptor-docking modules., Interleukin-2 (IL-2), which is one of the first cytokines identified and a member of the four-helix bundle cytokine superfamily, acts at the heart of the immune response (1). IL-2 and [...]
- Published
- 2005