Interleukin-17 Receptor A
The first IL-17 receptor (IL-17RA) was identified in 1995 by using the viral homolog, herpesvirus saimiri gene 13 (HVS13) (Yao et al. 1995). An Fc-HVS13 fusion protein was used to isolate cDNA from mouse T cells which encode a protein that binds all its orthologous forms. Following the discovery of mouse IL-17RA, Yao et al. isolated cDNA encoding the human IL-17RA from an activated peripheral blood leukocyte cDNA library by using mouse cDNA as a probe. The predicted 866-amino-acid type I membrane glycoprotein was 69% identical and 82% similar to the mouse sequence. It was not recognized to be related to any of the other known cytokine receptors and did not possess similarity to any other known protein nor any recognizable domains. Hence, IL-17RA and its ligand, IL-17A, represented a distinct highly conserved receptor-ligand pair. The study also showed low affinity of IL-17RA for IL-17A, lower than the concentration...
We apologize to those colleagues whose work, although relevant to the issues dealt within this chapter, has not been included due to space limitations. Also we appreciate OMIM (http://www.omim.org/) for the valuable compiled information. This work was supported by Grant no. 175062 from the Ministry of Education, Science and Technological Development of the Republic of Serbia.
- Zhang B, Liu C, Qian W, Han Y, Li X, Deng J. Structure of the unique SEFIR domain from human interleukin 17 receptor A reveals a composite ligand-binding site containing a conserved α-helix for Act1 binding and IL-17 signaling. Acta Crystallogr D Biol Crystallogr. 2014;70(Pt 5):1476–83.PubMedPubMedCentralCrossRefGoogle Scholar