1IRL

THE SOLUTION STRUCTURE OF THE F42A MUTANT OF HUMAN INTERLEUKIN 2

1IRL の概要

• エントリーDOI: 10.2210/pdb1irl/pdb
• 分子名称: INTERLEUKIN-2 (1 entity in total)
• 機能のキーワード: cytokine
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P60568
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15359.88

構造登録者

Mott, H.R.,Baines, B.S.,Hall, R.M.,Cooke, R.M.,Driscoll, P.C.,Weir, M.P.,Campbell, I.D. (登録日: 1995-08-25, 公開日: 1995-12-07, 最終更新日: 2024-10-23)

主引用文献

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

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: 7723044
DOI: 10.1006/jmbi.1994.0194

実験手法

SOLUTION NMR