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4EN0

Crystal structure of light

3UGN」から置き換えられました
4EN0 の概要
エントリーDOI10.2210/pdb4en0/pdb
分子名称Tumor necrosis factor ligand superfamily member 14, PHOSPHATE ION, GLYCEROL, ... (5 entities in total)
機能のキーワードstructural genomics, psi-biology, new york structural genomics research consortium, nysgrc, immunity, tnf superfamily, hvem, dcr3, n-glycosylation, membrane, secreted protein, cytokine, atoms-to-animals: the immune function network, ifn, jelly-roll fold, bind tnf receptor hvem and ltbr, ltbr
由来する生物種Homo sapiens (human)
タンパク質・核酸の鎖数3
化学式量合計55706.73
構造登録者
主引用文献Liu, W.,Zhan, C.,Cheng, H.,Kumar, P.R.,Bonanno, J.B.,Nathenson, S.G.,Almo, S.C.
Mechanistic basis for functional promiscuity in the TNF and TNF receptor superfamilies: structure of the LIGHT:DcR3 assembly.
Structure, 22:1252-1262, 2014
Cited by
PubMed Abstract: LIGHT initiates intracellular signaling via engagement of the two TNF receptors, HVEM and LTβR. In humans, LIGHT is neutralized by DcR3, a unique soluble member of the TNFR superfamily, which tightly binds LIGHT and inhibits its interactions with HVEM and LTβR. DcR3 also neutralizes two other TNF ligands, FasL and TL1A. Due to its ability to neutralize three distinct different ligands, DcR3 contributes to a wide range of biological and pathological processes, including cancer and autoimmune diseases. However, the mechanisms that support the broad specificity of DcR3 remain to be fully defined. We report the structures of LIGHT and the LIGHT:DcR3 complex, which reveal the structural basis for the DcR3-mediated neutralization of LIGHT and afford insights into DcR3 function and binding promiscuity. Based on these structures, we designed LIGHT mutants with altered affinities for DcR3 and HVEM, which may represent mechanistically informative probe reagents.
PubMed: 25087510
DOI: 10.1016/j.str.2014.06.013
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.59 Å)
構造検証レポート
Validation report summary of 4en0
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2024-11-06に公開中

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