Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments.

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.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Mott HR,Driscoll PC,Boyd J,Cooke RM,Weir MP,Campbell ID

doi

10.1021/bi00148a040

subject

Has Abstract

pub_date

1992-08-25 00:00:00

pages

7741-4

issue

33

eissn

0006-2960

issn

1520-4995

journal_volume

31

pub_type

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