| Literature DB >> 8786120 |
M Chérel1, M Sorel, F Apiou, B Lebeau, S Dubois, Y Jacques, S Minvielle.
Abstract
The high-affinity receptor for interleukin-11 (IL-11) is composed of two subunits, IL-11 receptor alpha chain (IL-11R alpha) and gp130, the common subunit of the interleukin-6 (IL-6), ciliary neurotrophic factor (CNTF), leukemia inhibitory factor, and oncostatin M receptors. The IL-11 receptor-specific alpha chain shares homologies with the alpha chain of the CNTF and IL-6 receptors. We isolated and characterized genomic DNA clones encompassing the entire coding sequence of the IL-11R alpha cDNA. The exon-intron organization of the IL-11R gene (HGMW-approved symbol IL11RA) is consistent with the predicted structure of the different domains of the IL-11R alpha protein, confirming evolutionary conservation at the level of gene organization among the hematopoietic cytokine receptor family. The IL-11R gene has been assigned to chromosome 9 band p13 by in situ hybridization using human IL-11R alpha cDNA as a probe. The fact that the ciliary neurotrophic factor (CNTFR) gene has recently been localized on this same band and the conserved genomic structure between IL-11R and CNTFR suggest that they may have evolved from a common ancestor.Entities:
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Year: 1996 PMID: 8786120 DOI: 10.1006/geno.1996.0075
Source DB: PubMed Journal: Genomics ISSN: 0888-7543 Impact factor: 5.736