1z92
From Proteopedia
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 disease associated with this structure: Severe combined immunodeficiency due to IL2 deficiency OMIM:[147680], Interleukin-2 receptor, alpha chain, deficiency of OMIM:[147730], Diabetes mellitus, insulin-dependent, susceptibility to, 10 OMIM:[147730]
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 Sat May 3 17:19:52 2008
