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Published online before print August 31, 2007, 10.1110/ps.072983507
Protein Science (2007), 16:2108-2117. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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Pre-structured motifs in the natively unstructured preS1 surface antigen of hepatitis B virus

Seung-Wook Chi1,3, Do-Hyoung Kim1,3, Si-Hyung Lee1, Iksoo Chang2, and Kyou-Hoon Han1

1 Molecular Cancer Research Center, Division of Molecular Therapeutics, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Korea
2 National Research Laboratory for Computational Proteomics and Biophysics, Department of Physics, Pusan National University, Pusan 609-735, Korea

(RECEIVED May 6, 2007; FINAL REVISION July 23, 2007; ACCEPTED July 25, 2007)

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 Pro32–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.

Keywords: hepatitis B virus; preS1; NMR; natively unstructured protein; pre-structured motif


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