Important note: Information in this article was accurate in 1985. The state of the art may have changed since the publication date.
Isolation and expression of complementary DNAs encoding the human interleukin 2 receptor.
Cancer Res. 1985 Sep;45(9 Suppl):4563s-4567s. Unique Identifier : AIDSLINE MED/85254471 Greene WC; Depper JM; Crabtree GR; Rudikoff S; Pumphrey J; Robb RJ; Kronke M; Svetlik P; Peffer NJ; Waldmann TA; et al
Abstract:
Complementary DNAs corresponding to the human receptor for interleukin 2 (IL-2) have been molecularly cloned, sequenced, and expressed in COS-1 cells. The human genome appears to contain a single structural gene for this receptor; however, when transcribed at least two messenger RNAs (mRNAs) are produced which vary in length due to the use of different polyadenylation signals. Sequence analysis of the cloned complementary DNAs indicates an alternate pathway of mRNA processing for this receptor. Splicing of a 216 base pairs segment contained within the protein coding region results in an mRNA unable to code for the IL-2 receptor. In contact complementary DNAs corresponding to unspliced mRNA encode membrane receptors which bind both IL-2 and anti-Tac (monoclonal anti-IL-2 receptor antibody). Analysis of the deduced amino acid sequence reveals that the receptor is composed of 272 amino acids including a signal peptide 21 amino acids in length. Hydrophobicity analysis suggests a single 19 amino acid transmembrane domain. A short intracytoplasmic domain composed of 13 amino acids is present at the carboxy terminus and contains three potential phosphate acceptor sites (serine and threonine but not tyrosine) and typical positively charged amino acids presumably involved in cytoplasmic anchoring. Two sites for N-linked glycosylation sites and numerous extracytoplasmic O-linked glycosylation sites are present.
Keywords: Amino Acid Sequence Base Sequence Cell Line Cell Transformation, Viral *Cloning, Molecular DNA/*GENETICS/ISOLATION & PURIF Genes, Structural Human HTLV-BLV Viruses/PHYSIOLOGY Interleukin-2/METABOLISM Nucleic Acid Hybridization Protein Processing, Post-Translational Receptors, Immunologic/BIOSYNTHESIS/*GENETICS/ISOLATION & PURIF/ METABOLISM RNA, Messenger/GENETICS JOURNAL ARTICLE
AEGiS is a 501(c)3, not-for-profit, tax-exempt, educational corporation. AEGiS is made possible through unrestricted funding from Bristol-Myers Squibb Company, Elton John AIDS Foundation, Gill Foundation, the National Library of Medicine, Quest Diagnostics, Roche and Trimeris, and donations from users like you. Always watch for outdated information. This article first appeared in 1985. This material is designed to support, not replace, the relationship that exists between you and your doctor.
AEGiS presents published material, reprinted with permission and neither endorses nor opposes any material. All information contained on this website, including information relating to health conditions, products, and treatments, is for informational purposes only. It is often presented in summary or aggregate form. It is not meant to be a substitute for the advice provided by your own physician or other medical professionals. Always discuss treatment options with a doctor who specializes in treating HIV.
Important note: Information in this article was accurate in 1985. The state of the art may have changed since the publication date.
