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2ILA

STRUCTURE OF INTERLEUKIN 1ALPHA AT 2.7-ANGSTROMS RESOLUTION

2ILA の概要
エントリーDOI10.2210/pdb2ila/pdb
分子名称INTERLEUKIN-1 ALPHA (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: P01583
タンパク質・核酸の鎖数1
化学式量合計17618.03
構造登録者
Graves, B.J.,Hatada, M.H. (登録日: 1991-05-01, 公開日: 1992-10-15, 最終更新日: 2024-02-21)
主引用文献Graves, B.J.,Hatada, M.H.,Hendrickson, W.A.,Miller, J.K.,Madison, V.S.,Satow, Y.
Structure of interleukin 1 alpha at 2.7-A resolution.
Biochemistry, 29:2679-2684, 1990
Cited by
PubMed Abstract: The interleukin 1 (IL-1) family of proteins has a central role in modulating immune and inflammatory responses. Two major IL-1 proteins, designated alpha (IL-1 alpha) and beta (IL-1 beta), are produced by activated macrophages and other cell types. In an effort to understand the similarities and differences in the physicochemical and functional properties of these two proteins, a program was initiated to determine their structures. Crystals of IL-1 alpha were grown, and the three-dimensional structure at 2.7-A resolution was solved. The technique of multiple-wavelength anomalous dispersion (MAD) with the selenomethionine form of IL-1 alpha was utilized in combination with a single mercury derivative to provide the starting phases. Partial refinement of the IL-1 alpha model has been performed as well. The overall structure is composed of 14 beta-strands and a 3(10) helix. The core of this structure is a capped beta-barrell that possesses 3-fold symmetry and displays a topology similar to that observed for IL-1 beta [Priestle, J. P., et al. (1988) EMBO J. 7, 339-343] and soybean trypsin inhibitor (STI) [McLachlan, A. D. (1979) J. Mol. Biol. 133, 557-563]. In this paper, the overall structure of IL-1 alpha and the nature and fidelity of the internal 3-fold symmetry are discussed. Comparisons with IL-1 beta and STI are made within these contexts.
PubMed: 2346741
DOI: 10.1021/bi00463a009
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.3 Å)
構造検証レポート
Validation report summary of 2ila
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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