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http://purl.uniprot.org/citations/34834922http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/34834922http://www.w3.org/2000/01/rdf-schema#comment"(1) Background: During maturation of the Hepatitis B virus, a viral polymerase inside the capsid transcribes a pre-genomic RNA into a partly double stranded DNA-genome. This is followed by envelopment with surface proteins inserted into a membrane. Envelopment is hypothetically regulated by a structural signal that reports the maturation state of the genome. NMR data suggest that such a signal can be mimicked by the binding of the detergent Triton X 100 to hydrophobic pockets in the capsid spikes. (2) Methods: We have used electron cryo-microscopy and image processing to elucidate the structural changes that are concomitant with the binding of Triton X 100. (3) Results: Our maps show that Triton X 100 binds with its hydrophobic head group inside the pocket. The hydrophilic tail delineates the outside of the spike and is coordinated via Lys-96. The binding of Triton X 100 changes the rotamer conformation of Phe-97 in helix 4, which enables a π-stacking interaction with Trp-62 in helix 3. Similar changes occur in mutants with low secretion phenotypes (P5T and L60V) and in a mutant with a pre-mature secretion phenotype (F97L). (4) Conclusion: Binding of Triton X 100 is unlikely to mimic structural maturation because mutants with different secretion phenotypes show similar structural responses."xsd:string
http://purl.uniprot.org/citations/34834922http://purl.org/dc/terms/identifier"doi:10.3390/v13112115"xsd:string
http://purl.uniprot.org/citations/34834922http://purl.uniprot.org/core/author"Bottcher B."xsd:string
http://purl.uniprot.org/citations/34834922http://purl.uniprot.org/core/author"Rasmussen T."xsd:string
http://purl.uniprot.org/citations/34834922http://purl.uniprot.org/core/author"Kraft C."xsd:string
http://purl.uniprot.org/citations/34834922http://purl.uniprot.org/core/author"Makbul C."xsd:string
http://purl.uniprot.org/citations/34834922http://purl.uniprot.org/core/author"Lappe M."xsd:string
http://purl.uniprot.org/citations/34834922http://purl.uniprot.org/core/author"Stohr M."xsd:string
http://purl.uniprot.org/citations/34834922http://purl.uniprot.org/core/author"Griessmann M."xsd:string
http://purl.uniprot.org/citations/34834922http://purl.uniprot.org/core/author"Katzenberger K."xsd:string
http://purl.uniprot.org/citations/34834922http://purl.uniprot.org/core/author"Pfarr P."xsd:string
http://purl.uniprot.org/citations/34834922http://purl.uniprot.org/core/author"Stoffer C."xsd:string
http://purl.uniprot.org/citations/34834922http://purl.uniprot.org/core/author"Wandinger A.M."xsd:string
http://purl.uniprot.org/citations/34834922http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/34834922http://purl.uniprot.org/core/name"Viruses"xsd:string
http://purl.uniprot.org/citations/34834922http://purl.uniprot.org/core/pages"2115"xsd:string
http://purl.uniprot.org/citations/34834922http://purl.uniprot.org/core/title"Binding of a Pocket Factor to Hepatitis B Virus Capsids Changes the Rotamer Conformation of Phenylalanine 97."xsd:string
http://purl.uniprot.org/citations/34834922http://purl.uniprot.org/core/volume"13"xsd:string
http://purl.uniprot.org/citations/34834922http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/34834922
http://purl.uniprot.org/citations/34834922http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/34834922
http://purl.uniprot.org/uniprot/#_P03146-mappedCitation-34834922http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34834922
http://purl.uniprot.org/uniprot/P03146http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34834922