The structure of human interleukin-11 reveals receptor-binding site features and structural differences from interleukin-6

TL Putoczki; RCJ Dobson; MDW Griffin

Journal article

The structure of human interleukin-11 reveals receptor-binding site features and structural differences from interleukin-6

TL Putoczki, RCJ Dobson, MDW Griffin

Acta Crystallographica Section D Biological Crystallography | Published : 2014

DOI: 10.1107/S1399004714012267

Abstract

Interleukin (IL)-11 is a multifunctional member of the IL-6 family of cytokines. Recombinant human IL-11 is administered as a standard clinical treatment for chemotherapy-induced thrombocytopaenia. Recently, a new role for IL-11 signalling as a potent driver of gastrointestinal cancers has been identified, and it has been demonstrated to be a novel therapeutic target for these diseases. Here, the crystal structure of human IL-11 is reported and the structural resolution of residues previously identified as important for IL-11 activity is presented. While IL-11 is thought to signal via a complex analogous to that of IL-6, comparisons show important differences between the two cytokines and it..

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University of Melbourne Researchers

Tracy Putoczki Author

Renwick Dobson Author

Michael Griffin Author

Related Projects (1)

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Grants

Awarded by Australian Research Council

Funding Acknowledgements

MDWG is the recipient of the C. R. Roper Fellowship and an Australian Research Council Postdoctoral Fellowship (project No. DP110103528). Parts of this research were undertaken at the MX2 and SAXS/WAXS beamlines of the Australian Synchrotron, Victoria, Australia. The authors wish to thank Professor Michael Parker for helpful advice and suggestions.