1IRL
THE SOLUTION STRUCTURE OF THE F42A MUTANT OF HUMAN INTERLEUKIN 2
Summary for 1IRL
| Entry DOI | 10.2210/pdb1irl/pdb |
| Descriptor | INTERLEUKIN-2 (1 entity in total) |
| Functional Keywords | cytokine |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted: P60568 |
| Total number of polymer chains | 1 |
| Total formula weight | 15359.88 |
| Authors | Mott, H.R.,Baines, B.S.,Hall, R.M.,Cooke, R.M.,Driscoll, P.C.,Weir, M.P.,Campbell, I.D. (deposition date: 1995-08-25, release date: 1995-12-07, Last modification date: 2024-10-23) |
| Primary citation | Mott, H.R.,Baines, B.S.,Hall, R.M.,Cooke, R.M.,Driscoll, P.C.,Weir, M.P.,Campbell, I.D. The solution structure of the F42A mutant of human interleukin 2. J.Mol.Biol., 247:979-994, 1995 Cited by PubMed Abstract: 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. PubMed: 7723044DOI: 10.1006/jmbi.1994.0194 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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