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

K. Albrandt, N. K. Orida, Fu-Tong Liu

Research output: Contribution to journalArticlepeer-review

103 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)6859-6863
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume84
Issue number19
StatePublished - Oct 1987

ASJC Scopus subject areas

  • General
  • Genetics

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