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© MPI f. Dynamik und Selbstorganisation
Publication : The Journal of biological chemistry

Structural analysis and modeling of a synthetic interleukin-2 mimetic and its interleukin-2Rbeta2 receptor

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The Journal of biological chemistry - 03 Apr 2003

Rose T, Moreau JL, Eckenberg R, Thèze J

Link to Pubmed [PMID] – 12676936

J. Biol. Chem. 2003 Jun;278(25):22868-76

Peptide p1-30, which is composed of the 30 amino-terminal residues (alpha-helix A) of human interleukin-2 (IL-2), binds as a tetramer to the dimeric IL-2Rbeta2 receptor, whereas the entire IL-2 recognizes the tricomponent receptor IL-2Ralphabetagamma. p1-30 is an IL-2 mimetic that activates CD8 low lymphocytes and natural killer cells, because these cells produce IL-2Rbeta constitutively. It also induces a strong lymphokine-activated killer cell response. A series of truncated peptides were analyzed by circular dichroism and analytical centrifugation to elucidate the role of p1-30 residues. We propose a model where residues 10-30 of the p1-30 peptide form an alpha-helix with eight hydrophobic side chains on the same surface buried in a hydrophobic core when four anti-parallel helices combine to form a bundle. IL-2Rbeta dimerization was further studied, and three-dimensional models of the free IL-2Rbeta2 receptor and the p1-304.IL-2Rbeta2 complex were built by comparative modeling based on the crystal structure of the erythropoietin receptor complex, because this belongs to the same hematopoietin family as IL-2. These models suggest that binding of the p1-30 tetramer rotates the COOH-terminal domains and brings both transmembrane regions 50 A closer together, driving the association of the two intracytoplasmic domains that would transduce the signal into the cytoplasm.

http://www.ncbi.nlm.nih.gov/pubmed/12676936