2b5i
From Proteopedia
cytokine receptor complex
Contents |
Overview
Interleukin-2 (IL-2) is an immunoregulatory cytokine that acts through a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors. In the structure of the quaternary ectodomain complex as visualized at a resolution of 2.3 angstroms, the binding of IL-2Ralpha to IL-2 stabilizes a secondary binding site for presentation to IL-2Rbeta. gammac is then recruited to the composite surface formed by the IL-2/IL-2Rbeta complex. Consistent with its role as a shared receptor for IL-4, IL-7, IL-9, IL-15, and IL-21, gammac forms degenerate contacts with IL-2. The structure of gammac provides a rationale for loss-of-function mutations found in patients with X-linked severe combined immunodeficiency diseases (X-SCID). This complex structure provides a framework for other gammac-dependent cytokine-receptor interactions and for the engineering of improved IL-2 therapeutics.
Disease
Known disease associated with this structure: Severe combined immunodeficiency due to IL2 deficiency OMIM:[147680], Combined immunodeficiency, X-linked, moderate OMIM:[308380], Severe combined immunodeficiency, X-linked OMIM:[308380], Interleukin-2 receptor, alpha chain, deficiency of OMIM:[147730], Diabetes mellitus, insulin-dependent, susceptibility to, 10 OMIM:[147730]
About this Structure
2B5I is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors., Wang X, Rickert M, Garcia KC, Science. 2005 Nov 18;310(5751):1159-63. PMID:16293754 Page seeded by OCA on Sat May 3 19:52:51 2008
