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1z92
From Proteopedia
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structure of interleukin-2 with its alpha receptor
Contents |
Overview
Interleukin-2 (IL-2) is an immunoregulatory cytokine that binds, sequentially to the alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma, chain (gammac) receptor subunits. Here we present the 2.8 angstrom crystal, structure of a complex between human IL-2 and IL-2Ralpha, which interact, in a docking mode distinct from that of other cytokine receptor complexes., IL-2Ralpha is composed of strand-swapped "sushi-like" domains, unlike the, classical cytokine receptor fold. As a result of this domain swap, IL-2Ralpha 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.
Disease
Known diseases associated with this structure: Diabetes mellitus, insulin-dependent, susceptibility to OMIM:[147730], Interleukin-2 receptor, alpha chain, deficiency of OMIM:[147730], Severe combined immunodeficiency due to IL2 deficiency OMIM:[147680]
About this Structure
1Z92 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structure of interleukin-2 complexed with its alpha receptor., Rickert M, Wang X, Boulanger MJ, Goriatcheva N, Garcia KC, Science. 2005 Jun 3;308(5727):1477-80. PMID:15933202
Page seeded by OCA on Mon Nov 12 20:31:13 2007
