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THE SOLUTION STRUCTURE OF THE F42A MUTANT OF HUMAN INTERLEUKIN 2
OverviewOverview
Interleukin 2 (IL-2) is one of the major cytokines produced by T, lymphocytes in response to antigen. It is a potent growth and, differentiation factor for several cell-types and is structurally related, to the four-helix bundle family of cytokines. Mutation of residue Phe42 to, Ala abolishes binding to the alpha chain of the tri-partite IL-2 receptor., The three-dimensional structure of the F42A mutant IL-2 has been, calculated by two dimensional NMR methods and compared to a structure of, wild-type IL-2 determined by X-ray crystallography. The overall topology, of the two structures is the same. The main differences between the, structures are within the ill-defined loops connecting the helices and the, region of the protein that is believed to interact with the alpha-chain of, the receptor. Thus, the mutation of Phe42 to Ala does not perturb the, overall three-dimensional structure of IL-2, and does not appear to change, the putative binding sites for the beta and gamma chains of the receptor., The structural differences observed in this mutant suggest that the, replacement of Phe42 with Ala causes the re-orientation of neighbouring, side-chains that are also involved in binding the alpha-chain of the, receptor.
DiseaseDisease
Known disease associated with this structure: Severe combined immunodeficiency due to IL2 deficiency OMIM:[147680]
About this StructureAbout this Structure
1IRL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
The solution structure of the F42A mutant of human interleukin 2., Mott HR, Baines BS, Hall RM, Cooke RM, Driscoll PC, Weir MP, Campbell ID, J Mol Biol. 1995 Apr 14;247(5):979-94. PMID:7723044
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