1MD6

High resolution crystal structure of murine IL-1F5 reveals unique loop conformation for specificity

1MD6 の概要

• エントリーDOI: 10.2210/pdb1md6/pdb
• 分子名称: interleukin 1 family, member 5 (delta) (2 entities in total)
• 機能のキーワード: beta triple, alpha helix, immune system
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Secreted (By similarity): Q9QYY1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16888.31

構造登録者

Pei, X.Y.,Dunn, E.F.,Gay, N.J.,O'Neill, L.A. (登録日: 2002-08-07, 公開日: 2003-09-30, 最終更新日: 2024-10-30)

主引用文献

Dunn, E.F.,Gay, N.J.,Bristow, A.F.,Gearing, D.P.,O'Neill, L.A.,Pei, X.Y.
High-Resolution Structure of Murine Interleukin 1 Homologue IL-1F5 Reveals Unique Loop Conformations for Receptor Binding Specificity.
Biochemistry, 42:10938-10944, 2003

PubMed Abstract: Interleukin-1 (IL-1) F5 is a novel member of the IL-1 family. The IL-1 family are involved in innate immune responses to infection and injury. These cytokines bind to specific receptors and cause activation of NFkappaB and MAP kinase. IL-1F5 has a sequence identity of 44% to IL-1 receptor antagonist (IL-1Ra), a natural antagonist of the IL-1 system. Here we report the crystal structure of IL-1F5 to a resolution of 1.6 A. It has the same beta-trefoil fold as other IL-1 family members, and the hydrophobic core is well conserved. However, there are substantial differences in the loop conformations, structures that confer binding specificity for the cognate receptor to IL-1beta and the antagonist IL-1Ra. Docking and superimposition of the IL-1F5 structure suggest that is unlikely to bind to the interleukin1 receptor, consistent with biochemical studies. The structure IL-1F5 lacks features that confer antagonist properties on IL-1Ra, and we predict that like IL-1beta it will act as an agonist. These studies give insights into how distinct receptor specificities can evolve within related cytokine families.

PubMed: 12974628
DOI: 10.1021/bi0341197

実験手法

X-RAY DIFFRACTION (1.6 Å)