ArticleProtein science : a publication of the Protein Society2007
Pre-structured motifs in the natively unstructured preS1 surface antigen of hepatitis B virus.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Multistep receptor binding of the hepatitis B virus preS1 domain.Nature communications · 2026Article
- Structural basis of hepatitis B virus receptor binding.Nature structural & molecular biology · 2024Article
- α-Linolenic Acid Vesicles-Mediated Tau Internalization in Microglia.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Biochemical and Biophysical Characterization of Tau and α-Linolenic Acid Vesicles In Vitro.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Article
- Choice of Force Field for Proteins Containing Structured and Intrinsically Disordered Regions.Biophysical journal · 2020Article
- Phosphorylation and Alternative Translation on Wheat Germ Cell-Free Protein Synthesis of the DHBV Large Envelope Protein.Frontiers in molecular biosciences · 2019Article
- Transient Secondary Structures as General Target-Binding Motifs in Intrinsically Disordered Proteins.International journal of molecular sciences · 2018Review
- PreSMo Target-Binding Signatures in Intrinsically Disordered Proteins.Molecules and cells · 2018Review
- An NMR study on the intrinsically disordered core transactivation domain of human glucocorticoid receptor.BMB reports · 2017Article
- Efficient Inhibition of Hepatitis B Virus Infection by a preS1-binding Peptide.Scientific reports · 2016Article
- Inhibition of preS1-hepatocyte interaction by an array of recombinant human antibodies from naturally recovered individuals.Scientific reports · 2016Article
- Applications of human hepatitis B virus preS domain in bio- and nanotechnology.World journal of gastroenterology · 2015Review
- Intrinsically disordered proteins in the nucleus of human cells.Biochemistry and biophysics reports · 2015Article
- The intrinsic disorder alphabet. III. Dual personality of serine.Intrinsically disordered proteins · 2015Review
- The hepatitis B virus preS1 domain hijacks host trafficking proteins by motif mimicry.Nature chemical biology · 2013Article
- The twenty-year story of a plant-based vaccine against hepatitis B: stagnation or promising prospects?International journal of molecular sciences · 2013Review
- Structures of hepatitis B virus cores presenting a model epitope and their complexes with antibodies.Journal of molecular biology · 2012Article
- Structural characterization of an intrinsically unfolded mini-HBX protein from hepatitis B virus.Molecules and cells · 2012Article
- The functional and structural characterization of a novel oncogene GIG47 involved in the breast tumorigenesis.BMC cancer · 2012Article
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5 authors.
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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)-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.
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