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Pre‐structured motifs in the natively unstructured preS1 surface antigen of hepatitis B virus
Author(s) -
Chi SeungWook,
Kim DoHyoung,
Lee SiHyung,
Chang Iksoo,
Han KyouHoon
Publication year - 2007
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.072983507
Subject(s) - heteronuclear molecule , hepatitis b virus , chemistry , protein secondary structure , hbsag , computational biology , virus , biochemistry , biology , stereochemistry , virology , nuclear magnetic resonance spectroscopy
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 –Ala 36 and Pro 41 –Phe 45 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.