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a ligand peptide motif selected from a cancer patient is a receptor-interacting site within human interleukin-11配体肽主题选择从一个癌症病人是人类interleukin-11 receptor-interacting站点内.pdf

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a ligand peptide motif selected from a cancer patient is a receptor-interacting site within human interleukin-11配体肽主题选择从一个癌症病人是人类interleukin-11 receptor-interacting站点内

A Ligand Peptide Motif Selected from a Cancer Patient Is a Receptor-Interacting Site within Human Interleukin-11 ´ 1 1 1 1 1 Marina Cardo-Vila , Amado J. Zurita , Ricardo J. Giordano , Jessica Sun , Roberto Rangel , Liliana 1 2 2 ´ 2 1 Guzman-Rojas , Cristiane D. Anobom , Ana P. Valente , Fabio C. L. Almeida , Johanna Lahdenranta , 1 1 1 Mikhail G. Kolonin , Wadih Arap *, Renata Pasqualini * 1The University of Texas M. D. Anderson Cancer Center, Houston, Texas, United States of America, 2 National NMR Center, Federal University, Rio de Janeiro, Brazil Abstract Interleukin-11 (IL-11) is a pleiotropic cytokine approved by the FDA against chemotherapy-induced thrombocytopenia. From a combinatorial selection in a cancer patient, we isolated an IL-11-like peptide mapping to domain I of the IL-11 (sequence CGRRAGGSC). Although this motif has ligand attributes, it is not within the previously characterized interacting sites. Here we design and validate in-tandem binding assays, site-directed mutagenesis and NMR spectroscopy to show (i) the peptide mimics a receptor-binding site within IL-11, (ii) the binding of CGRRAGGSC to the IL-11Ra is functionally relevant, (iii) Arg4 and Ser8 are the key residues mediating the interaction, and (iv) the IL-11-like motif induces cell proliferation through STAT3 activation. These structural and functional results uncover an as yet unrecognized receptor- binding site in human IL-11. Given that IL-11Ra has been proposed as