[PreSMo_doi]
doi:10.20927/presmo.112406
[PreSMo_Name]
preS1 of HBV-pre6
[PreSMo_Residues]
α Helix 46-50
[Role]
Hepatocyte receptor binding
[Species]
Hepatitis B Virus
[YearFound_Released]
2007
[Reporter]
Kyou-Hoon Han
[Description]
null
[IDP_Name]
preS1 of HBV
[Link]
http://www.doi.or.kr/wordpress/?p=1715
[Residue_count]
119
[Amino_Seq]
Met1Gly2Gly2Trp4Ser5Ser6Lys7Pro8Arg9Gln10Gly11Met12Gly13Thr14Asn15Leu16Ser17Val18Pro19Asn20Pro21Leu22Gly23Phe24Phe25Pro26Asp27His28Gln29Leu30Asp31Pro32Ala33Phe34Gly35Ala36Asn37Ser38Asn39Asn40Pro41Asp42Trp43Asp44Phe45Asn46Pro47Asn48Lys49Asp50His51Trp52Pro5
[Reference]
doi:10.1110/ps.072983507
Pre-structured motifs in the natively unstructured preS1 surface antigen of hepatitis B virus

Seung-Wook Chi, Do-Hyoung Kim, Si-Hyung Lee, Iksoo Chang, and Kyou-Hoon Han

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.


[Structure]