The crystal structure of human glycosylation-inhibiting factor is a trimeric barrel with three 6-stranded β-sheets

Yoichi Kato, Takanori Muto, Takafumi Tomura, Haruhiko Tsumura, Hiroshi Watarai, Toshifumi Mikayama, Kimishige Ishizaka, Ryota Kuroki

Research output: Contribution to journalArticle

Abstract

Glycosylation-inhibiting factor (GIF) is a cytokine that is involved in the regulation of IgE synthesis. The crystal structure of recombinant human GIF was determined by the multiple isomorphous replacement method. The structure was refined to an R factor of 0.168 at 1.9 Å resolution. The overall structure is seen to consist of three interconnected subunits forming a barrel with three 6-stranded β-sheets on the inside and six α-helices on the outside. There is o 5-Å-diameter 'hole' through the middle of the barrel. The barrel structure of GIF in part resembles other 'trefoil' cytokines such as interleukin 1 and fibroblast growth factor. Each subunit has a new class of α + β sandwich structure consisting of two β-α-β motifs. These β-α-β motifs are related by a pseudo-twofold axis and resemble both interleukin 8 and the peptide binding domain of major histocompatibility complex protein, although the topology of the polypeptide chain is quite different.

Original languageEnglish (US)
Pages (from-to)3007-3010
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume93
Issue number7
DOIs
StatePublished - Apr 2 1996

Keywords

  • cytokine
  • multiple isomorphous replacement
  • x-ray crystallography
  • α + β sandwich structure

ASJC Scopus subject areas

  • General

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