1BXT

STREPTOCOCCAL SUPERANTIGEN (SSA) FROM STREPTOCOCCUS PYOGENES

1BXT の概要

• エントリーDOI: 10.2210/pdb1bxt/pdb
• 分子名称: PROTEIN (STREPTOCOCCAL SUPERANTIGEN) (2 entities in total)
• 機能のキーワード: bacterial superantigen, mhc class ii interaction, t cell activation, toxic shock-like syndrome, immune system
• 由来する生物種: Streptococcus pyogenes
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53908.57

構造登録者

Sundberg, E.,Jardetzky, T. (登録日: 1998-10-08, 公開日: 1998-10-14, 最終更新日: 2024-11-20)

主引用文献

Sundberg, E.,Jardetzky, T.S.
Structural basis for HLA-DQ binding by the streptococcal superantigen SSA.
Nat.Struct.Biol., 6:123-129, 1999

PubMed Abstract: Streptococcal superantigen (SSA) is a 28,000 Mr toxin originally isolated from a pathogenic strain of Streptococcus pyogenes that has 60% sequence identity with staphylococcal enterotoxin B (SEB). SSA and SEB, however, do not compete for binding on the surfaces of cells expressing MHC class II molecules. This behavior had been ascribed to SSA and SEB binding to distinct sites on, or different subsets of, HLA-DR molecules. Here we demonstrate that SSA binds predominantly to HLA-DQ, rather than to HLA-DR molecules, and present the crystal structure of SSA at 1.85 A resolution. These data provide a structural basis for interpreting the interaction of SSA with HLA-DQ molecules as well as a foundation for understanding bacterial superantigen affinities for distinct MHC isotypes.

PubMed: 10048922
DOI: 10.1038/5809

実験手法

X-RAY DIFFRACTION (1.85 Å)