4ZF7
Crystal structure of ferret interleukin-2
Summary for 4ZF7
Entry DOI | 10.2210/pdb4zf7/pdb |
Descriptor | Interleukin 2, SULFATE ION, TETRAETHYLENE GLYCOL, ... (6 entities in total) |
Functional Keywords | ferret, interleukin-2, immune system |
Biological source | Mustela putorius furo (European domestic ferret) |
Cellular location | Secreted : A3FBE6 |
Total number of polymer chains | 2 |
Total formula weight | 33079.84 |
Authors | Ren, B.,Newman, J.,McKinstry, W.J.,Adams, T.E. (deposition date: 2015-04-21, release date: 2015-11-04, Last modification date: 2024-10-30) |
Primary citation | Ren, B.,McKinstry, W.J.,Pham, T.,Newman, J.,Layton, D.S.,Bean, A.G.,Chen, Z.,Laurie, K.L.,Borg, K.,Barr, I.G.,Adams, T.E. Structural and functional characterisation of ferret interleukin-2. Dev.Comp.Immunol., 55:32-38, 2015 Cited by PubMed Abstract: While the ferret is a valuable animal model for a number of human viral infections, such as influenza, Hendra and Nipah, evaluating the cellular immune response following infection has been hampered by the lack of a number of species-specific immunological reagents. Interleukin 2 (IL-2) is one such key cytokine. Ferret recombinant IL-2 incorporating a C-terminal histidine tag was expressed and purified and the three-dimensional structure solved and refined at 1.89 Å by X-ray crystallography, which represents the highest resolution and first non-human IL-2 structure. While ferret IL-2 displays the classic cytokine fold of the four-helix bundle structure, conformational flexibility was observed at the second helix and its neighbouring region in the bundle, which may result in the disruption of the spatial arrangement of residues involved in receptor binding interactions, implicating subtle differences between ferret and human IL-2 when initiating biological functions. Ferret recombinant IL-2 stimulated the proliferation of ferret lymph node cells and induced the expression of mRNA for IFN-γ and Granzyme A. PubMed: 26472619DOI: 10.1016/j.dci.2015.10.007 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.893 Å) |
Structure validation
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