1BBN
THREE-DIMENSIONAL SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-4 BY MULTI-DIMENSIONAL HETERONUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
1BBN の概要
エントリーDOI | 10.2210/pdb1bbn/pdb |
分子名称 | INTERLEUKIN-4 (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: P05112 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 15391.60 |
構造登録者 | Clore, G.M.,Powers, B.,Garrett, D.S.,Gronenborn, A.M. (登録日: 1992-05-01, 公開日: 1993-10-31, 最終更新日: 2024-10-16) |
主引用文献 | Powers, R.,Garrett, D.S.,March, C.J.,Frieden, E.A.,Gronenborn, A.M.,Clore, G.M. Three-dimensional solution structure of human interleukin-4 by multidimensional heteronuclear magnetic resonance spectroscopy. Science, 256:1673-1677, 1992 Cited by PubMed Abstract: The three-dimensional solution structure of recombinant human interleukin-4, a protein of 133 residues and 15.4 kilodaltons that plays a key role in the immune and inflammatory systems, has been solved by multidimensional heteronuclear magnetic resonance spectroscopy. The structure is dominated by a left-handed four-helix bundle with an unusual topology comprising two overhand connections. The linker elements between the helices are formed by either long loops, small helical turns, or short strands. The overall topology is remarkably similar to that of growth hormone and granulocyte-macrophage colony stimulating factor, despite the absence of any sequence homology, and substantial differences in the relative lengths of the helices, the length and nature of the various connecting elements, and the pattern of disulfide bridges. These three proteins, however, bind to cell surface receptors belonging to the same hematopoietic superfamily, which suggests that interleukin-4 may interact with its receptor in an analogous manner to that observed in the crystal structure of the growth hormone-extracellular receptor complex. PubMed: 1609277主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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