1md6
From Proteopedia
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High resolution crystal structure of murine IL-1F5 reveals unique loop conformation for specificity
Overview
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.
About this Structure
1MD6 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
High-resolution structure of murine interleukin 1 homologue IL-1F5 reveals unique loop conformations for receptor binding specificity., Dunn EF, Gay NJ, Bristow AF, Gearing DP, O'Neill LA, Pei XY, Biochemistry. 2003 Sep 23;42(37):10938-44. PMID:12974628
Page seeded by OCA on Tue Nov 20 21:20:23 2007
