Journal of the Korean Magnetic Resonance Society (한국자기공명학회논문지)

Korean Magnetic Resonance Society (한국자기공명학회)
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Structural characterization of HBx-interacting protein using NMR spectroscopy

  • Lee Young-Tae (Department of Chemistry and National Creative Research Initiative Center, Korea Advanced Institute of Science and Technology) ;
  • Kim Byoung-Kook (Department of Chemistry and National Creative Research Initiative Center, Korea Advanced Institute of Science and Technology) ;
  • Kim Key-Sun (Biomedical Research Center, Korea Institute of Science and Technology) ;
  • Choi Byong-Seok (Department of Chemistry and National Creative Research Initiative Center, Korea Advanced Institute of Science and Technology)
  • Published : 2005.12.01
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Abstract

The hepatitis B virus X protein (HBx) is highly linked with liver diseases and the development of hepatocellular carcinoma. HBx-interacting protein (XIP) has been shown to abolish the transactivation functions of HBx. Here, we define the structural characteristics and HBx binding properties of XIP. Under physiological conditions, XIP was composed mainly of random-coils but significant helicity was induced in the hydrophobic condition. NMR spectroscopy defined the secondary structure of XIP in the presence of sodium dodecyl sulfate. Four putative helices were mapped to the amino acids 8-12, 32-38, 42-54 and 82-91. Any deletion of defined putative helices in XIP led to loss of binding to HBx, and truncated mutant lacking last putative helix decreased helicity more than that it could. Our results suggest that XIP requires its entire sequence for HBx binding and it may be under drastic conformational change when binds to HBx.

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