Unique structural features of flaviviruses’ capsid proteins: new insights on structure-function relationship
| Autor: | Ícaro Putinhon Caruso, Fabio C. L. Almeida, Thais Cristtina Neves-Martins, Nathane C. Mebus-Antunes, Andrea T. Da Poian |
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| Rok vydání: | 2021 |
| Předmět: |
Protein Conformation
alpha-Helical 0301 basic medicine viruses Static Electricity 030106 microbiology Computational biology Genome Dengue fever Structure-Activity Relationship 03 medical and health sciences Flaviviridae Virology medicine Humans Protein Structure Quaternary biology Flavivirus RNA Nuclear magnetic resonance spectroscopy biology.organism_classification medicine.disease 030104 developmental biology Capsid Helix Capsid Proteins Protein crystallization Protein Binding |
| Zdroj: | Current Opinion in Virology. 47:106-112 |
| ISSN: | 1879-6257 |
| Popis: | The Flaviviridae family comprises important human pathogens, including Dengue, Zika, West Nile, Yellow Fever and Japanese Encephalitis viruses. The viral genome, a positive-sense single-stranded RNA, is packaged by a single protein, the capsid protein, which is a small and highly basic protein that form intertwined homodimers in solution. Atomic-resolution structures of four flaviviruses capsid proteins were solved either in solution by nuclear magnetic resonance spectroscopy, or after protein crystallization by X-ray diffraction. Analyses of these structures revealed very particular properties, namely (i) the predominance of quaternary contacts maintaining the structure; (ii) a highly electropositive surface throughout the protein; and (iii) a flexible helix (α1). The goal of this review is to discuss the role of these features in protein structure-function relationship. |
| Databáze: | OpenAIRE |
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