<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>20(16)</volume><submitter>Faustino AF</submitter><pubmed_abstract>Dengue, West Nile and Zika, closely related viruses of the Flaviviridae family, are an increasing global threat, due to the expansion of their mosquito vectors. They present a very similar viral particle with an outer lipid bilayer containing two viral proteins and, within it, the nucleocapsid core. This core is composed by the viral RNA complexed with multiple copies of the capsid protein, a crucial structural protein that mediates not only viral assembly, but also encapsidation, by interacting with host lipid systems. The capsid is a homodimeric protein that contains a disordered N-terminal region, an intermediate flexible fold section and a very stable conserved fold region. Since a better understanding of its structure can give light into its biological activity, here, first, we compar</pubmed_abstract><journal>International journal of molecular sciences</journal><pagination>E3870</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6720645</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Structural and Functional Properties of the Capsid Protein of Dengue and Related Flavivirus.</pubmed_title><pmcid>PMC6720645</pmcid><pubmed_authors>Artilheiro V</pubmed_authors><pubmed_authors>Karguth N</pubmed_authors><pubmed_authors>Enguita FJ</pubmed_authors><pubmed_authors>Ricardo JC</pubmed_authors><pubmed_authors>Martins AS</pubmed_authors><pubmed_authors>Faustino AF</pubmed_authors><pubmed_authors>Santos NC</pubmed_authors><pubmed_authors>Martins IC</pubmed_authors></additional><is_claimable>false</is_claimable><name>Structural and Functional Properties of the Capsid Protein of Dengue and Related Flavivirus.</name><description>Dengue, West Nile and Zika, closely related viruses of the Flaviviridae family, are an increasing global threat, due to the expansion of their mosquito vectors. They present a very similar viral particle with an outer lipid bilayer containing two viral proteins and, within it, the nucleocapsid core. This core is composed by the viral RNA complexed with multiple copies of the capsid protein, a crucial structural protein that mediates not only viral assembly, but also encapsidation, by interacting with host lipid systems. The capsid is a homodimeric protein that contains a disordered N-terminal region, an intermediate flexible fold section and a very stable conserved fold region. Since a better understanding of its structure can give light into its biological activity, here, first, we compar</description><dates><release>2019-01-01T00:00:00Z</release><publication>2019 Aug</publication><modification>2025-04-04T20:48:01.943Z</modification><creation>2019-09-24T07:06:40Z</creation></dates><accession>S-EPMC6720645</accession><cross_references><pubmed>31398956</pubmed><doi>10.3390/ijms20163870</doi></cross_references></HashMap>