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- Pre-structured motifs in the natively unstructured preS1 surface antigen of hepatitis B virus
- Seung-Wook Chi; Do-heyoung Kim; Si Hyung Lee; I Chang; Kyou Hoon Han
- Bibliographic Citation
- Protein Science, vol. 16, no. 10, pp. 2108-2117
- Publication Year
- The preS1 surface antigen of hepatitis B virus (HBV) is known to play an important role in the initial attachment of HBV to hepatocytes. We have characterized structural features of the full-length preS1 using heteronuclear NMR methods and discovered that this 119-residue protein is inherently unstructured without a unique tertiary structure under a nondenaturing condition. Yet, combination of various NMR parameters shows that the preS1 contains "pre-structured" domains broadly covering its functional domains. The most prominent domain is formed by residues 27-45 and overlaps with the putative hepatocyte-binding domain (HBD) encompassing residues 21-47, within which two well-defined pre-structured motifs, formed by Pro 32-Ala36 and Pro41-Phe45 are found. Additional, somewhat less prominent, pre-structured motifs are also formed by residues 11-18, 22-25, 37-40, and 46-50. Overall results suggest that the preS1 is a natively unstructured protein (NUP) whose N-terminal 50 residues, populated with multiple pre-structured motifs, contribute critically to hepatocyte binding.
- hepatitis B virus; natively unstructured protein; NMR; pre-structured motif; preS1
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- Division of Biomedical Research > 1. Journal Articles
Division of Bio Technology Innovation > Core Facility Management Center > 1. Journal Articles
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