An IgE-binding protein with a distinctive repetitive sequence and homology with an IgG receptor

Proc Natl Acad Sci U S A. 1987 Oct;84(19):6859-63. doi: 10.1073/pnas.84.19.6859.

Abstract

Proteins that bind IgE play important roles in both the synthesis and function of IgE are therefore intimately involved in IgE-mediated human allergic disorders. This report describes the structure of an IgE-binding protein, as predicted from sequencing a cDNA cloned from rat basophilic leukemia cells. This protein contains two domains: the amino-terminal domain (140 amino acids) consists of a highly conserved repetitive amino acid sequence, Tyr-Pro-Gly-Pro/Gln-Ala/Thr-Pro/Ala-Pro-Gly-Ala, whereas the carboxyl-terminal domain (122 amino acids) shares significant sequence homology with a domain of lymphocyte/macrophage receptor for the Fc portion of IgG. Other proteins with this type of structure but with affinity for other immunoglobulin isotypes may exist and may represent a heretofore unidentified component of the immune system.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cell Line
  • Immunoglobulin E / immunology*
  • Immunoglobulin G / immunology*
  • Molecular Sequence Data
  • Receptors, Fc / genetics*
  • Receptors, IgE
  • Receptors, IgG
  • Repetitive Sequences, Nucleic Acid

Substances

  • Immunoglobulin G
  • Receptors, Fc
  • Receptors, IgE
  • Receptors, IgG
  • Immunoglobulin E

Associated data

  • GENBANK/J02962