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Structural characterization of HBx-interacting protein using NMR spectroscopy

김기선|김병국|최병석|이영태
한국자기공명학회 (Korean Magnetic Resonance Society)|2005.12|Journal of the Korean Magnetic Resonance Society|제9권 제2호|pp. 122-137

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참고문헌

키워드

NMRHBxXIPnatively unfolded protein
주제분류화학

초록

The hepatitis B virus X protein (HBx) is highly linked with liver diseases and the development of hepatocellular carcinoma. HBxinteracting 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. Key words: HBx, XIP, NMR, natively unfolded protein

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.

참고문헌 (29)

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