The Drosophila EGF receptor gene homolog: Conservation of both hormone binding and kinase domains

Etta Livneh, Lillian Glazer, Daniel Segal, Joseph Schlessinger, Ben Zion Shilo

Research output: Contribution to journalArticlepeer-review

135 Scopus citations

Abstract

Chicken v-erbB probe was used to isolate a unique clone of Drosophila melanogaster DNA. It maps by in situ hybridization to position 57F on chromosome 2. A complete nucleotide sequence of the coding region has been obtained. The putative Drosophila EGF receptor protein is similar in overall organization to the human homolog. It shows three distinct domains: an extracellular putative EGF binding domain, a hydrophobic transmembrane region, and a cytoplasmic kinase domain. The overall amino acid homology is 41% in the extracellular domain and 55% in the kinase domain. Two cysteine-rich regions, a hallmark of the human ligand-binding domain, have also been conserved. Fusion of the coding sequences of the kinase and extracellular domains generating the receptor gene must have occurred over 800 million years ago.

Original languageEnglish
Pages (from-to)599-607
Number of pages9
JournalCell
Volume40
Issue number3
DOIs
StatePublished - 1 Jan 1985
Externally publishedYes

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