4MHL

The crystal structure of human interleukin-11

Summary for 4MHL

• Entry DOI: 10.2210/pdb4mhl/pdb
• Descriptor: Interleukin-11, SULFATE ION, FORMAMIDE, ... (4 entities in total)
• Functional Keywords: four-helix bundle, long-chain helical cytokine, cytokine, growth factor, interleukin-11 receptor subunit alpha, membrane glycoprotein 130, secreted, protein binding
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P20809
• Total number of polymer chains: 1
• Total formula weight: 19393.52

Authors

Griffin, M.D.W. (deposition date: 2013-08-29, release date: 2014-09-03, Last modification date: 2023-09-20)

Primary citation

Putoczki, T.L.,Dobson, R.C.,Griffin, M.D.
The structure of human interleukin-11 reveals receptor-binding site features and structural differences from interleukin-6.
Acta Crystallogr.,Sect.D, 70:2277-2285, 2014

PubMed 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 is suggested that IL-11 engages GP130 differently to IL-6. In addition to providing a structural platform for further study of IL-11, these data offer insight into the binding interactions of IL-11 with each of its receptors and the structural mechanisms underlying agonist and antagonist variants of the protein.

PubMed: 25195742
DOI: 10.1107/S1399004714012267

Experimental method

X-RAY DIFFRACTION (2.09 Å)