1IFA
THREE-DIMENSIONAL CRYSTAL STRUCTURE OF RECOMBINANT MURINE INTERFERON-BETA
1IFA の概要
| エントリーDOI | 10.2210/pdb1ifa/pdb |
| 分子名称 | INTERFERON-BETA, ASPARAGINE (2 entities in total) |
| 機能のキーワード | glycoprotein |
| 由来する生物種 | Mus musculus (house mouse) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 19551.68 |
| 構造登録者 | Mitsui, Y.,Senda, T.,Matsuda, S.,Kawano, G.,Nakamura, K.T.,Shimizu, H. (登録日: 1991-10-29, 公開日: 1994-01-31, 最終更新日: 2024-02-07) |
| 主引用文献 | Senda, T.,Shimazu, T.,Matsuda, S.,Kawano, G.,Shimizu, H.,Nakamura, K.T.,Mitsui, Y. Three-dimensional crystal structure of recombinant murine interferon-beta. EMBO J., 11:3193-3201, 1992 Cited by PubMed Abstract: The crystal structure of recombinant murine interferon-beta (IFN-beta) has been solved by the multiple isomorphous replacement method and refined to an R-factor of 20.5% against 2.6 A X-ray diffraction data. The structure shows a variant of the alpha-helix bundle with a new chain-folding topology, which seems to represent a basic structural framework of all the IFN-alpha and IFN-beta molecules belonging to the type I family. Functionally important segments of the polypeptide chain, as implied through numerous gene manipulation studies carried out so far, are spatially clustered indicating the binding site(s) to the receptor(s). Comparison of the present structure with those of other alpha-helical cytokine proteins, including porcine growth hormone, interleukin 2 and interferon gamma, indicated either a topological similarity in chain folding or a similar spatial arrangement of the alpha-helices. PubMed: 1505514主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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