| Literature DB >> 2404337 |
N Itoh1, S Yonehara, J Schreurs, D M Gorman, K Maruyama, A Ishii, I Yahara, K Arai, A Miyajima.
Abstract
Interleukin-3 (IL-3) binds to its receptor with high and low affinities, induces tyrosine phosphorylation, and promotes the proliferation and differentiation of hematopoietic cells. A binding component of the IL-3 receptor was cloned. Fibroblasts transfected with the complementary DNA bound IL-3 with a low affinity [dissociation constant (Kd) of 17.9 +/- 3.6 nM]. No consensus sequence for a tyrosine kinase was present in the cytoplasmic domain. Thus, additional components are required for a functional high affinity IL-3 receptor. A sequence comparison of the IL-3 receptor with other cytokine receptors (erythropoietin, IL-4, IL-6, and the beta chain IL-2 receptor) revealed a common motif of a distinct receptor gene family.Entities:
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Year: 1990 PMID: 2404337 DOI: 10.1126/science.2404337
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728