Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments.
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.
Mott
H R
HR
Department of Biochemistry, University of Oxford, U.K.
Driscoll
P C
PC
Boyd
J
J
Cooke
R M
RM
Weir
M P
MP
Campbell
I D
ID
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D016178:Granulocyte-Macrophage Colony-Stimulating Factor / Q000737:chemistry; D006801:Humans; D007376:Interleukin-2 / Q000737:chemistry*; D015847:Interleukin-4 / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008961:Models, Structural; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
D007376:Interleukin-2; D009587:Nitrogen Isotopes; D011994:Recombinant Proteins; D015847:Interleukin-4; D016178:Granulocyte-Macrophage Colony-Stimulating Factor