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6KRY

Structure of staphylococcal enterotoxin SEN

6KRY の概要
エントリーDOI10.2210/pdb6kry/pdb
分子名称Enterotoxin SEN variant (2 entities in total)
機能のキーワードstaphylococcal enterotoxin, sen, allergen
由来する生物種Staphylococcus aureus
タンパク質・核酸の鎖数1
化学式量合計26145.22
構造登録者
Han, Z.,Zeng, C. (登録日: 2019-08-22, 公開日: 2019-12-04, 最終更新日: 2024-03-27)
主引用文献Zeng, C.,Liu, Z.,Han, Z.
Structure of Staphylococcal Enterotoxin N: Implications for Binding Properties to Its Cellular Proteins.
Int J Mol Sci, 20:-, 2019
Cited by
PubMed Abstract: strains produce a unique family of immunostimulatory exotoxins termed as bacterial superantigens (SAgs), which cross-link major histocompatibility complex class II (MHC II) molecule and T-cell receptor (TCR) to stimulate large numbers of T cells at extremely low concentrations. SAgs are associated with food poisoning and toxic shock syndrome. To date, 26 genetically distinct staphylococcal SAgs have been reported. This study reports the first X-ray structure of newly characterized staphylococcal enterotoxin N (SEN). SEN possesses the classical two domain architecture that includes an N-terminal oligonucleotide-binding fold and a C-terminal β-grasp domain. Amino acid and structure alignments revealed that several critical amino acids that are proposed to be responsible for MHC II and TCR molecule engagements are variable in SEN, suggesting that SEN may adopt a different binding mode to its cellular receptors. This work helps better understand the mechanisms of action of SAgs.
PubMed: 31775346
DOI: 10.3390/ijms20235921
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.8 Å)
構造検証レポート
Validation report summary of 6kry
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2024-10-30に公開中

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