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Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments
H R Mott1, P C Driscoll, J Boyd
1Department of Biochemistry, University of Oxford, U.K.
Biochemistry
|August 25, 1992
Abstract:
Recombinant 15N-labeled human interleukin 2 (IL-2) has been studied by 2D and 3D NMR using uniformly 15N-labeled protein. Assignment of the backbone resonances has enabled the secondary structure of the protein to be defined. The secondary structure was found to consist of four alpha-helical regions and a short section of antiparallel beta-sheet. This structure is more similar to recent published structures of interleukin 4 and granulocyte-macrophage colony-stimulating factor than to a structure of IL-2 previously obtained from low-resolution X-ray diffraction data.