Protein Family Models

The E. coli interleukin [IL] receptor mimic protein A (IrmA), is a small (13 kDa) Uropathogenic E. coli (UPEC) protein that was originally identified in a large reverse genetic screen as a broadly protective vaccine antigen. It has a fibronectin III (FNIII)-like fold that forms a domain-swapped dimer with structural mimicry to the binding domain of the IL-2 receptor (IL-2R), the IL-4 receptor (IL-4R) and, to a lesser extent, the IL-10 receptor (IL-10R). IrmA binds to all three cytokines, with the greatest affinity observed for IL-4. It is suggested that IrmA may contribute to manipulation of the innate immune response during UPEC infection [1]. [1]. 26980835. Molecular and Structural Characterization of a Novel Escherichia coli Interleukin Receptor Mimic Protein. Moriel DG, Heras B, Paxman JJ, Lo AW, Tan L, Sullivan MJ, Dando SJ, Beatson SA, Ulett GC, Schembri MA;. MBio. 2016;7:e02046. (from Pfam)

Date:

2024-10-16