이영태 Kim, Byoung kook 김기선 최병석 2024-01-21T04:03:44Z 2024-01-21T04:03:44Z 2021-09-06 2005-12 1226-6531 https://pubs.kist.re.kr/handle/201004/135933 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 English 한국자기공명학회 Structural characterization of HBx-interacting protein using NMR spectroscopy Article 2 Journal of the Korean Magnetic Resonance Society, v.9, no.2, pp.122 - 137 Journal of the Korean Magnetic Resonance Society 9 2 122 137 N kci other ART001177888 HBx XIP NMR natively unfolded protein