Molecular characterization of a new immunoglobulin superfamily protein with potential roles in opioid binding and cell contact

P. R. Schofield, K. C. McFarland, J. S. Hayflick, J. N. Wilcox, T. M. Cho, S. Roy, N. M. Lee, H. H. Loh, P. H. Seeburg

Research output: Contribution to journalArticle

94 Scopus citations

Abstract

A purified opioid-binding protein has been characterized by cDNA cloning. The cDNA sequence predicts an extracellularly located glycoprotein of 345 amino acids. This protein does not possess a membrane-spanning domain but contains a C-terminal hydrophobic sequence characteristic of membrane attachment by a phosphatidylinositol linkage. It displays homology to the immunoglobulin protein superfamily, featuring three domains that resemble disulfide-bonded constant regions. More specifically, the protein is most homologous to a subfamily of proteins which includes the neural cell adhesion molecule (NCAM) and myelin-associated glycoprotein (MAG) and one subgroup of the tyrosine kinase growth factor receptors comprising the platelet-derived growth factor receptor (PDGF R), the colony-stimulating factor 1 receptor (CSF-1 R) ahd the c-kit protooncogene. These sequence homologies suggest that the protein could be involved in either cell recognition and adhesion, peptidergic ligand binding or both.

Original languageEnglish (US)
Pages (from-to)489-495
Number of pages7
JournalEMBO Journal
Volume8
Issue number2
DOIs
StatePublished - 1989

Fingerprint Dive into the research topics of 'Molecular characterization of a new immunoglobulin superfamily protein with potential roles in opioid binding and cell contact'. Together they form a unique fingerprint.

  • Cite this