{"doi":"10.1126/science.286.5438.287","title":"X-ray Crystallographic Structure of the Norwalk Virus Capsid","abstract":"<jats:p>Norwalk virus, a noncultivatable human calicivirus, is the major cause of epidemic gastroenteritis in humans. The first x-ray structure of a calicivirus capsid, which consists of 180 copies of a single protein, has been determined by phase extension from a low-resolution electron microscopy structure. The capsid protein has a protruding (P) domain connected by a flexible hinge to a shell (S) domain that has a classical eight-stranded β-sandwich motif. The structure of the P domain is unlike that of any other viral protein with a subdomain exhibiting a fold similar to that of the second domain in the eukaryotic translation elongation factor–Tu. This subdomain, located at the exterior of the capsid, has the largest sequence variation among Norwalk-like human caliciviruses and is likely to contain the determinants of strain specificity and cell binding.</jats:p>","journal":"Science","year":1999,"id":17127,"datarank":16.979376673501577,"base_score":6.8690144506657065,"endowment":6.8690144506657065,"self_citation_contribution":1.0303521675998562,"citation_network_contribution":15.949024505901722,"self_endowment_contribution":1.0303521675998562,"citer_contribution":15.949024505901722,"corpus_percentile":null,"corpus_rank":null,"citation_count":961,"citer_count":200,"citers_with_citation_signal":200,"citers_with_endowment":200,"datacite_reuse_total":24,"is_dataset":false,"is_dataset_confidence":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":123614,"name":"Michele E. Hardy","orcid":null,"position":1,"is_corresponding":false},{"id":123615,"name":"Terje Dokland","orcid":null,"position":2,"is_corresponding":false},{"id":123616,"name":"Jordi Bella","orcid":null,"position":3,"is_corresponding":false},{"id":91658,"name":"Michael G. Rossmann","orcid":"0000-0002-9468-9309","position":4,"is_corresponding":false},{"id":123617,"name":"Mary K. Estes","orcid":null,"position":5,"is_corresponding":false},{"id":123613,"name":"B. V. V. Prasad","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":6.8690144506657065,"endowment":6.8690144506657065,"datacite_reuse_total":24,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"10514371","pmcid":null,"openalex_id":"https://openalex.org/W2130788389","authors":[],"funders":[],"total_grants":0,"fwci":8.9808,"citation_percentile":0.98522841,"influential_citations":69,"citation_trend":[{"year":2012,"count":41},{"year":2013,"count":49},{"year":2014,"count":53},{"year":2015,"count":55},{"year":2016,"count":45},{"year":2017,"count":36},{"year":2018,"count":43},{"year":2019,"count":53},{"year":2020,"count":41},{"year":2021,"count":65},{"year":2022,"count":39},{"year":2023,"count":36},{"year":2024,"count":37},{"year":2025,"count":37},{"year":2026,"count":10}],"oa_status":"closed","license":null,"oa_locations":[{"url":"https://www.science.org/doi/pdf/10.1126/science.286.5438.287","host_type":"publisher"},{"url":"https://doi.org/10.1126/science.286.5438.287","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/10514371","host_type":"repository"},{"url":"https://research.manchester.ac.uk/en/publications/7fb7dc56-74fe-4a04-b99c-31a69cfe9cc6","host_type":"repository"},{"url":"https://www.research.manchester.ac.uk/portal/en/publications/xray-crystallographic-structure-of-the-norwalk-virus-capsid(7fb7dc56-74fe-4a04-b99c-31a69cfe9cc6).html","host_type":"repository"}],"fields_of_study":["Viral gastroenteritis research and epidemiology","Viral Infections and Immunology Research","Bacteriophages and microbial interactions","Biology","Medicine","Amino Acid Sequence","Capsid","Capsid Proteins","Cryoelectron Microscopy","Crystallography, X-Ray","Dimerization","Genome, Viral","Humans","Hydrogen Bonding","Image Processing, Computer-Assisted","Models, Molecular","Molecular Sequence Data","Norwalk virus","Protein Conformation","Protein Folding","Protein Structure, Secondary","Recombinant Proteins","Virus Assembly"],"mesh_terms":["Amino Acid Sequence","Capsid","Humans","Hydrogen Bonding","Image Processing, Computer-Assisted","Models, Molecular","Molecular Sequence Data","Norwalk virus","Protein Conformation","Recombinant Proteins","Genome, Viral","Protein Structure, Secondary","Protein Folding","Crystallography, X-Ray","Virus Assembly","Dimerization","Cryoelectron Microscopy","Capsid Proteins"],"keywords":["Capsid","Norwalk virus","Calicivirus","Feline calicivirus","Caliciviridae","Virology","Biology","Parvoviridae","Virus","Viral protein","Crystallography","Parvovirus","Chemistry","Viral disease"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Good health and well-being"}],"linked_datasets":[{"doi":"10.6084/m9.figshare.13558411.v1","title":"Additional file 1 of Broad-range and effective detection of human noroviruses by colloidal gold immunochromatographic assay based on the shell domain of the major capsid protein","publisher":"figshare","resource_type":"JournalArticle"},{"doi":"10.6084/m9.figshare.13558411","title":"Additional file 1 of Broad-range and effective detection of human noroviruses by colloidal gold immunochromatographic assay based on the shell domain of the major capsid protein","publisher":"figshare","resource_type":"JournalArticle"},{"doi":"10.6084/m9.figshare.13558414.v1","title":"Additional file 2 of Broad-range and effective detection of human noroviruses by colloidal gold immunochromatographic assay based on the 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