Interleukin Structure


Structure is an important and useful character to classify evolutionarily related proteins. For interleukin, IL1-like cytokines can be identified from other cytokines by a fold rich in beta-strands. IL6, IL11, IL12A, IL23A, IL27A, IL31 and oncostatin M (OSM) are long-chain class I helical cytokines. However, IL2, IL3, IL4, IL5, IL7, IL9, IL13, IL15 and IL21 are short-chain helical cytokines. The IL10-like and IL28-like are similar in structure through a fold that contains six or seven stacked α-helices. IL17 family members are structurally unrelated to other IL subfamily. IL17F shares a high degree of sequence homology with IL17A. IL17F was recently crystalized and structural analysis, finding a cysteine-knot fold.

 

Related literatures

1. Brocker C, Thompson D, Matsumoto A, Nebert DW, Vasiliou V. "Evolutionary divergence and functions of the human interleukin (IL) gene family.". Human Genomics 5 (1): 30–55, OCTOBER 2010.

2. Commins, S.P., Borish, L. and Steinke, J.W. (2010), ‘Immunologic messenger molecules: Cytokines, interferons, and chemokines’, J. Allergy Clin. Immunol. Vol. 125, pp. S53–S72.

IL12 receptors