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Crystal Structure of the TNF-α-Inducing Protein (Tipα) fromHelicobacter pylori: Insights into Its DNA-Binding Activity

Authors
Journal
Journal of Molecular Biology
0022-2836
Publisher
Elsevier
Publication Date
Volume
392
Issue
1
Identifiers
DOI: 10.1016/j.jmb.2009.07.010
Keywords
  • Tumor Necrosis Factor-α-Inducing Protein
  • Tipα
  • Hp0596
  • Helicobacter Pylori
  • Gastric Cancer
Disciplines
  • Biology
  • Medicine

Abstract

Abstract Helicobacter pylori infection is one of the highest risk factors for gastroduodenal diseases including gastric cancer. Tumor necrosis factor-alpha (TNF-α) is one of the essential cytokines for tumor promotion, and thus, an H. pylori protein that induces TNF-α is believed to play a significant role in gastric cancer development in humans. The HP0596 gene product of H. pylori strain 26695 was identified as the TNF-α-inducing protein (Tipα). Tipα is secreted from H. pylori as dimers and enters the gastric cells. It was shown to have a DNA-binding activity. Here, we have determined the crystal structure of Tipα from H. pylori. Its monomer consists of two structural domains (“mixed domain” and “helical domain”). Tipα exists as a dimer in the crystal, and the dimeric structure represents a novel scaffold for DNA binding. A positively charged surface patch formed across the two monomers of the Tipα dimer by the loop between helices α1 and α2 may be important in DNA binding.

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