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Title 

Pre-structured motifs in the natively unstructured preS1 surface antigen of hepatitis B virus

Authors 

Seung-Wook ChiDo-heyoung KimSi Hyung LeeI ChangKyou Hoon Han

Publisher 

Cold Spring Harbor Laboratory Press

Issue Date 

2007

Citation 

Protein Science, vol. 16, no. 10, pp. 2108-2117

Keywords 

hepatitis B virusnatively unstructured proteinNMRpre-structured motifpreS1hepatitis B surface antigenmembrane proteinpreS1 surface proteinprotein precursorvirus protein

Abstract 

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.

ISSN 

0961-8368

Link 

http://dx.doi.org/10.1110/ps.072983507

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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