5UUI

Crystal Structure of Spin-Labeled T77C TNFa

5UUI の概要

• エントリーDOI: 10.2210/pdb5uui/pdb
• 分子名称: Tumor necrosis factor, S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate (3 entities in total)
• 機能のキーワード: t77c, tnfa, tnf alpha, cytokine, immune system
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Cell membrane ; Single-pass type II membrane protein . Tumor necrosis factor, membrane form: Membrane; Single-pass type II membrane protein. Tumor necrosis factor, soluble form: Secreted. C-domain 1: Secreted. C-domain 2: Secreted: P01375
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17724.16

構造登録者

Horanyi, P.S.,Dranow, D.M.,Ceska, T. (登録日: 2017-02-16, 公開日: 2017-08-02, 最終更新日: 2024-10-16)

主引用文献

Carrington, B.,Myers, W.K.,Horanyi, P.,Calmiano, M.,Lawson, A.D.G.
Natural Conformational Sampling of Human TNF alpha Visualized by Double Electron-Electron Resonance.
Biophys. J., 113:371-380, 2017

PubMed Abstract: Double electron-electron resonance in conjunction with site-directed spin labeling has been used to probe natural conformational sampling of the human tumor necrosis factor α trimer. We suggest a previously unreported, predeoligomerization conformation of the trimer that has been shown to be sampled at low frequency. A model of this trimeric state has been constructed based on crystal structures using the double-electron-electron-resonance distances. The model shows one of the protomers to be rotated and tilted outward at the tip end, leading to a breaking of the trimerous symmetry and distortion at a receptor-binding interface. The new structure offers opportunities to modulate the biological activity of tumor necrosis factor α through stabilization of the distorted trimer with small molecules.

PubMed: 28746848
DOI: 10.1016/j.bpj.2017.06.007

実験手法

X-RAY DIFFRACTION (1.4 Å)